Protein-coding gene in the species Homo sapiens
TBP
Available structures
PDB Ortholog search:
PDBe
RCSB List of PDB id codes
1TGH ,
1C9B ,
1JFI ,
1NVP ,
4ROC ,
4ROE ,
4ROD ,
5IY9 ,
5IYA ,
5FUR ,
5IYC ,
5IYB ,
5IY7 ,
5IY8 ,
5IYD ,
5IY6
Identifiers
Aliases
TBP , GTF2D, GTF2D1, HDL4, SCA17, TFIID, TATA-box binding protein, TATA-binding protein, TBP1External IDs
OMIM :
600075
MGI :
101838
HomoloGene :
2404
GeneCards :
TBP
Wikidata
The TATA-binding protein (TBP ) is a
general transcription factor that binds to a
DNA sequence called the
TATA box . This DNA sequence is found about 30
base pairs upstream of the
transcription start site in some
eukaryotic
gene
promoters .
[5]
TBP gene family
TBP is a member of a small gene family of TBP-related factors.
[6] The first TBP-related factor (TRF/TRF1) was identified in the fruit fly
Drosophila , but appears to be fly or insect-specific. Subsequently
TBPL1 /TRF2 was found in the genomes of many
metazoans , whereas
vertebrate genomes encode a third vertebrate family member,
TBPL2 /TRF3. In specific cell types or on specific promoters TBP can be replaced by one of these TBP-related factors, some of which interact with the TATA box similarly to TBP.
Role as transcription factor
TBP is a subunit of the eukaryotic
general transcription factor
TFIID . TFIID is the first protein to bind to DNA during the formation of the
transcription preinitiation complex of
RNA polymerase II (RNA Pol II).
[7] As one of the few proteins in the preinitiation complex that binds DNA in a sequence-specific manner, it helps position RNA polymerase II over the
transcription start site of the gene. However, it is estimated that only 10–20% of human promoters have TATA boxes - the majority of human promoters are
TATA -less
housekeeping gene
promoters - so TBP is probably not the only protein involved in positioning RNA polymerase II.. The binding of TBP to these promoters is facilitated by housekeeping gene regulators.
[8]
[9] Interestingly, transcription initiates within a narrow region at around 30 bp downstream of TATA box on TATA-containing promoters,
[10] while transcription start sites of TATA-less promoters are dispersed within a 200 bp region.
[11]
[9]
Binding of TFIID to the
TATA box in the
promoter region of the gene initiates the recruitment of other factors required for RNA Pol II to begin transcription. Some of the other recruited transcription factors include
TFIIA ,
TFIIB , and
TFIIF . Each of these transcription factors contains several protein subunits.
TBP is also important for transcription by
RNA polymerase I and
RNA polymerase III , and is therefore involved in transcription initiation by all three RNA polymerases.
[12]
TBP is involved in
DNA melting (double strand separation) by bending the
DNA by 80° (the AT-rich sequence to which it binds facilitates easy melting). The TBP is an unusual protein in that it binds the minor groove using a β sheet.
Another distinctive feature of TBP is a long string of glutamines in the N-terminus of the protein. This region modulates the DNA binding activity of the C-terminus, and modulation of DNA-binding affects the rate of transcription complex formation and initiation of transcription. Mutations that expand the number of CAG repeats encoding this
polyglutamine tract , and thus increase the length of the polyglutamine string, are associated with
spinocerebellar ataxia 17, a
neurodegenerative disorder classified as a
polyglutamine disease .
[13]
DNA-protein interactions
When TBP binds to a
TATA box within the
DNA , it distorts the DNA by inserting amino acid side-chains between base pairs, partially unwinding the helix, and doubly kinking it. The distortion is accomplished through a great amount of surface contact between the protein and DNA. TBP binds with the negatively charged phosphates in the DNA backbone through positively charged
lysine and
arginine amino acid residues. The sharp bend in the DNA is produced through projection of four bulky
phenylalanine residues into the minor groove. As the DNA bends, its contact with TBP increases, thus enhancing the DNA-protein interaction.
The strain imposed on the DNA through this interaction initiates melting, or separation, of the strands. Because this region of DNA is rich in
adenine and
thymine residues, which base-pair through only two
hydrogen bonds , the DNA strands are more easily separated. Separation of the two strands exposes the bases and allows
RNA polymerase II to begin transcription of the
gene .
TBP's C-terminus composes of a helicoidal shape that (incompletely) complements the T-A-T-A region of DNA. This incompleteness allows DNA to be passively bent on binding.
For information on the use of TBP in cells see:
RNA polymerase I ,
RNA polymerase II , and
RNA polymerase III .
Protein–protein interactions
TATA-binding protein has been shown to
interact with:
BRF1 ,
[14]
[15]
BTAF1 ,
[16]
[17]
C-Fos ,
[18]
C-jun ,
[19]
EDF1 ,
[20]
[21]
[22]
GTF2B (TFIIB),
[23]
[24]
GTF2A1 (
TFIIA subunit 1),
[23]
[25]
[26]
[27]
GTF2F1 (
TFIIF subunit 1)
[16]
[28]
[29]
GTF2H4 (
TFIIH subunit 4),
[16]
Mdm2 ,
[30]
[31]
MSX1 ,
[32]
[33]
[34]
NFYB ,
[35]
P53 ,
[36]
[37]
PAX6 ,
[37]
POLR2A ,
[16]
POU2F1 ,
[38]
RELA ,
[39]
[40]
NR2B1 ,
[41]
TAF1 ,
[35]
[42]
[43]
[44]
TAF4 ,
[45]
TAF5 ,
[35]
[43]
[46]
TAF6 ,
[35]
[43]
[45]
TAF7 ,
[35]
[45]
TAF9 .
[35]
[47]
TAF10 ,
[35]
[43]
TAF11 ,
[35]
[48]
[49]
TAF13 ,
[48] and
TAF15 .
[50]
Complex assembly
The TATA-box
binding
protein (TBP) is required for the initiation of
transcription by RNA
polymerases I, II and III, from
promoters with or without a TATA box.
[51]
[52] In the presence of a TATA-less promoter, TBP binds with the help of TBP-associated factors (TAFs).
[53]
[54] TBP associates with a host of factors, including the general
transcription factors TFIIA, -B, -D, -E, and -H, to form huge multi-subunit pre-initiation complexes on the core
promoter . Through its association with different
transcription factors, TBP can initiate
transcription from different RNA
polymerases . There are several related TBPs, including TBP-like (TBPL)
proteins .
[55]
Structure
The C-terminal core of TBP (~180 residues) is
highly conserved and contains two 88-amino acid
repeats that produce a saddle-shaped
structure that straddles the DNA; this region
binds to the TATA box and
interacts with
transcription factors and
regulatory
proteins .
[56] By contrast, the N-terminal region varies in both length and
sequence .
References
^
a
b
c
GRCh38: Ensembl release 89: ENSG00000112592 –
Ensembl , May 2017
^
a
b
c
GRCm38: Ensembl release 89: ENSMUSG00000014767 –
Ensembl , May 2017
^
"Human PubMed Reference:" . National Center for Biotechnology Information, U.S. National Library of Medicine .
^
"Mouse PubMed Reference:" . National Center for Biotechnology Information, U.S. National Library of Medicine .
^ Kornberg RD (2007).
"The molecular basis of eukaryotic transcription" . Proc. Natl. Acad. Sci. U.S.A . 104 (32): 12955–61.
Bibcode :
2007PNAS..10412955K .
doi :
10.1073/pnas.0704138104 .
PMC
1941834 .
PMID
17670940 .
^ Akhtar W, Veenstra GJ (1 January 2011).
"TBP-related factors: a paradigm of diversity in transcription initiation" . Cell & Bioscience . 1 (1): 23.
doi :
10.1186/2045-3701-1-23 .
PMC
3142196 .
PMID
21711503 .
^ Lee TI, Young RA (2000). "Transcription of eukaryotic protein-coding genes". Annual Review of Genetics . 34 : 77–137.
doi :
10.1146/annurev.genet.34.1.77 .
PMID
11092823 .
^ Lam KC, Mühlpfordt F, Vaquerizas JM, Raja SJ, Holz H, Luscombe NM, Manke T, Akhtar A (2012).
"The NSL complex regulates housekeeping genes in Drosophila" . PLOS Genetics . 8 (6): e1002736.
doi :
10.1371/journal.pgen.1002736 .
PMC
3375229 .
PMID
22723752 .
^
a
b Lam KC, Chung HR, Semplicio G, Iyer SS, Gaub A, Bhardwaj V, Holz H, Georgiev P, Akhtar A (February 2019).
"The NSL complex-mediated nucleosome landscape is required to maintain transcription fidelity and suppression of transcription noise" . Genes & Development . 33 (7–8): 452–465.
doi :
10.1101/gad.321489.118 .
PMC
6446542 .
PMID
30819819 .
^ Carninci P, Sandelin A, Lenhard B, Katayama S, Shimokawa K, Ponjavic J, et al. (June 2006). "Genome-wide analysis of mammalian promoter architecture and evolution". Nature Genetics . 38 (6): 626–35.
doi :
10.1038/ng1789 .
PMID
16645617 .
S2CID
22205897 .
^ Ni T, Corcoran DL, Rach EA, Song S, Spana EP, Gao Y, Ohler U, Zhu J (July 2010).
"A paired-end sequencing strategy to map the complex landscape of transcription initiation" . Nature Methods . 7 (7): 521–7.
doi :
10.1038/nmeth.1464 .
PMC
3197272 .
PMID
20495556 .
^ Vannini A, Cramer P (February 2012).
"Conservation between the RNA polymerase I, II, and III transcription initiation machineries" . Molecular Cell . 45 (4): 439–46.
doi :
10.1016/j.molcel.2012.01.023 .
hdl :
11858/00-001M-0000-0015-483A-5 .
PMID
22365827 .
^
"Entrez Gene: TBP TATA box binding protein" .
^ McCulloch V, Hardin P, Peng W, Ruppert JM, Lobo-Ruppert SM (August 2000).
"Alternatively spliced hBRF variants function at different RNA polymerase III promoters" . EMBO J . 19 (15): 4134–43.
doi :
10.1093/emboj/19.15.4134 .
PMC
306597 .
PMID
10921893 .
^ Wang Z, Roeder RG (July 1995).
"Structure and function of a human transcription factor TFIIIB subunit that is evolutionarily conserved and contains both TFIIB- and high-mobility-group protein 2-related domains" . Proc. Natl. Acad. Sci. U.S.A . 92 (15): 7026–30.
Bibcode :
1995PNAS...92.7026W .
doi :
10.1073/pnas.92.15.7026 .
PMC
41464 .
PMID
7624363 .
^
a
b
c
d Scully R, Anderson SF, Chao DM, Wei W, Ye L, Young RA, Livingston DM, Parvin JD (May 1997).
"BRCA1 is a component of the RNA polymerase II holoenzyme" . Proc. Natl. Acad. Sci. U.S.A . 94 (11): 5605–10.
Bibcode :
1997PNAS...94.5605S .
doi :
10.1073/pnas.94.11.5605 .
PMC
20825 .
PMID
9159119 .
^ Chicca JJ, Auble DT, Pugh BF (March 1998).
"Cloning and biochemical characterization of TAF-172, a human homolog of yeast Mot1" . Mol. Cell. Biol . 18 (3): 1701–10.
doi :
10.1128/MCB.18.3.1701 .
PMC
108885 .
PMID
9488487 .
^ Metz R, Bannister AJ, Sutherland JA, Hagemeier C, O'Rourke EC, Cook A, Bravo R, Kouzarides T (September 1994).
"c-Fos-induced activation of a TATA-box-containing promoter involves direct contact with TATA-box-binding protein" . Mol. Cell. Biol . 14 (9): 6021–9.
doi :
10.1128/MCB.14.9.6021 .
PMC
359128 .
PMID
8065335 .
^ Franklin CC, McCulloch AV, Kraft AS (February 1995).
"In vitro association between the Jun protein family and the general transcription factors, TBP and TFIIB" . Biochem. J . 305 (3): 967–74.
doi :
10.1042/bj3050967 .
PMC
1136352 .
PMID
7848298 .
^ Brendel C, Gelman L, Auwerx J (June 2002).
"Multiprotein bridging factor-1 (MBF-1) is a cofactor for nuclear receptors that regulate lipid metabolism" . Mol. Endocrinol . 16 (6): 1367–77.
doi :
10.1210/mend.16.6.0843 .
PMID
12040021 .
^ Mariotti M, De Benedictis L, Avon E, Maier JA (August 2000).
"Interaction between endothelial differentiation-related factor-1 and calmodulin in vitro and in vivo" . J. Biol. Chem . 275 (31): 24047–51.
doi :
10.1074/jbc.M001928200 .
PMID
10816571 .
^ Kabe Y, Goto M, Shima D, Imai T, Wada T, Morohashi Ki, Shirakawa M, Hirose S, Handa H (November 1999).
"The role of human MBF1 as a transcriptional coactivator" . J. Biol. Chem . 274 (48): 34196–202.
doi :
10.1074/jbc.274.48.34196 .
PMID
10567391 .
^
a
b Tang H, Sun X, Reinberg D,
Ebright RH (February 1996).
"Protein–protein interactions in eukaryotic transcription initiation: structure of the preinitiation complex" . Proc. Natl. Acad. Sci. U.S.A . 93 (3): 1119–24.
Bibcode :
1996PNAS...93.1119T .
doi :
10.1073/pnas.93.3.1119 .
PMC
40041 .
PMID
8577725 .
^ Bushnell DA, Westover KD, Davis RE, Kornberg RD (February 2004). "Structural basis of transcription: an RNA polymerase II-TFIIB cocrystal at 4.5 Angstroms". Science . 303 (5660): 983–8.
Bibcode :
2004Sci...303..983B .
doi :
10.1126/science.1090838 .
PMID
14963322 .
S2CID
36598301 .
^ DeJong J, Bernstein R, Roeder RG (April 1995).
"Human general transcription factor TFIIA: characterization of a cDNA encoding the small subunit and requirement for basal and activated transcription" . Proc. Natl. Acad. Sci. U.S.A . 92 (8): 3313–7.
Bibcode :
1995PNAS...92.3313D .
doi :
10.1073/pnas.92.8.3313 .
PMC
42156 .
PMID
7724559 .
^ Ozer J, Mitsouras K, Zerby D, Carey M, Lieberman PM (June 1998).
"Transcription factor IIA derepresses TATA-binding protein (TBP)-associated factor inhibition of TBP-DNA binding" . J. Biol. Chem . 273 (23): 14293–300.
doi :
10.1074/jbc.273.23.14293 .
PMID
9603936 .
^ Sun X, Ma D, Sheldon M, Yeung K, Reinberg D (October 1994).
"Reconstitution of human TFIIA activity from recombinant polypeptides: a role in TFIID-mediated transcription" . Genes Dev . 8 (19): 2336–48.
doi :
10.1101/gad.8.19.2336 .
PMID
7958900 .
^ Ruppert S, Tjian R (November 1995).
"Human TAFII250 interacts with RAP74: implications for RNA polymerase II initiation" . Genes Dev . 9 (22): 2747–55.
doi :
10.1101/gad.9.22.2747 .
PMID
7590250 .
^ Malik S, Guermah M, Roeder RG (March 1998).
"A dynamic model for PC4 coactivator function in RNA polymerase II transcription" . Proc. Natl. Acad. Sci. U.S.A . 95 (5): 2192–7.
Bibcode :
1998PNAS...95.2192M .
doi :
10.1073/pnas.95.5.2192 .
PMC
19292 .
PMID
9482861 .
^ Thut CJ, Goodrich JA, Tjian R (August 1997).
"Repression of p53-mediated transcription by MDM2: a dual mechanism" . Genes Dev . 11 (15): 1974–86.
doi :
10.1101/gad.11.15.1974 .
PMC
316412 .
PMID
9271120 .
^ Léveillard T, Wasylyk B (December 1997).
"The MDM2 C-terminal region binds to TAFII250 and is required for MDM2 regulation of the cyclin A promoter" . J. Biol. Chem . 272 (49): 30651–61.
doi :
10.1074/jbc.272.49.30651 .
PMID
9388200 .
^ Shetty S, Takahashi T, Matsui H, Ayengar R, Raghow R (May 1999).
"Transcriptional autorepression of Msx1 gene is mediated by interactions of Msx1 protein with a multi-protein transcriptional complex containing TATA-binding protein, Sp1 and cAMP-response-element-binding protein-binding protein (CBP/p300)" . Biochem. J . 339 (3): 751–8.
doi :
10.1042/0264-6021:3390751 .
PMC
1220213 .
PMID
10215616 .
^ Zhang H, Hu G, Wang H, Sciavolino P, Iler N, Shen MM, Abate-Shen C (May 1997).
"Heterodimerization of Msx and Dlx homeoproteins results in functional antagonism" . Mol. Cell. Biol . 17 (5): 2920–32.
doi :
10.1128/mcb.17.5.2920 .
PMC
232144 .
PMID
9111364 .
^ Zhang H, Catron KM, Abate-Shen C (March 1996).
"A role for the Msx-1 homeodomain in transcriptional regulation: residues in the N-terminal arm mediate TATA binding protein interaction and transcriptional repression" . Proc. Natl. Acad. Sci. U.S.A . 93 (5): 1764–9.
Bibcode :
1996PNAS...93.1764Z .
doi :
10.1073/pnas.93.5.1764 .
PMC
39855 .
PMID
8700832 .
^
a
b
c
d
e
f
g
h Bellorini M, Lee DK, Dantonel JC, Zemzoumi K, Roeder RG, Tora L, Mantovani R (June 1997).
"CCAAT binding NF-Y-TBP interactions: NF-YB and NF-YC require short domains adjacent to their histone fold motifs for association with TBP basic residues" . Nucleic Acids Res . 25 (11): 2174–81.
doi :
10.1093/nar/25.11.2174 .
PMC
146709 .
PMID
9153318 .
^ Seto E, Usheva A, Zambetti GP, Momand J, Horikoshi N, Weinmann R, Levine AJ, Shenk T (December 1992).
"Wild-type p53 binds to the TATA-binding protein and represses transcription" . Proc. Natl. Acad. Sci. U.S.A . 89 (24): 12028–32.
Bibcode :
1992PNAS...8912028S .
doi :
10.1073/pnas.89.24.12028 .
PMC
50691 .
PMID
1465435 .
^
a
b Cvekl A, Kashanchi F, Brady JN, Piatigorsky J (June 1999). "Pax-6 interactions with TATA-box-binding protein and retinoblastoma protein". Invest. Ophthalmol. Vis. Sci . 40 (7): 1343–50.
PMID
10359315 .
^ Zwilling S, Annweiler A, Wirth T (May 1994).
"The POU domains of the Oct1 and Oct2 transcription factors mediate specific interaction with TBP" . Nucleic Acids Res . 22 (9): 1655–62.
doi :
10.1093/nar/22.9.1655 .
PMC
308045 .
PMID
8202368 .
^ Guermah M, Malik S, Roeder RG (June 1998).
"Involvement of TFIID and USA components in transcriptional activation of the human immunodeficiency virus promoter by NF-kappaB and Sp1" . Mol. Cell. Biol . 18 (6): 3234–44.
doi :
10.1128/mcb.18.6.3234 .
PMC
108905 .
PMID
9584164 .
^ Schmitz ML, Stelzer G, Altmann H, Meisterernst M, Baeuerle PA (March 1995).
"Interaction of the COOH-terminal transactivation domain of p65 NF-kappa B with TATA-binding protein, transcription factor IIB, and coactivators" . J. Biol. Chem . 270 (13): 7219–26.
doi :
10.1074/jbc.270.13.7219 .
PMID
7706261 .
^ Schulman IG, Chakravarti D, Juguilon H, Romo A, Evans RM (August 1995).
"Interactions between the retinoid X receptor and a conserved region of the TATA-binding protein mediate hormone-dependent transactivation" . Proc. Natl. Acad. Sci. U.S.A . 92 (18): 8288–92.
Bibcode :
1995PNAS...92.8288S .
doi :
10.1073/pnas.92.18.8288 .
PMC
41142 .
PMID
7667283 .
^ Siegert JL, Robbins PD (January 1999).
"Rb inhibits the intrinsic kinase activity of TATA-binding protein-associated factor TAFII250" . Mol. Cell. Biol . 19 (1): 846–54.
doi :
10.1128/MCB.19.1.846 .
PMC
83941 .
PMID
9858607 .
^
a
b
c
d Ruppert S, Wang EH, Tjian R (March 1993).
"Cloning and expression of human TAFII250: a TBP-associated factor implicated in cell-cycle regulation" . Nature . 362 (6416): 175–9.
Bibcode :
1993Natur.362..175R .
doi :
10.1038/362175a0 .
PMID
7680771 .
S2CID
4364676 .
^ O'Brien T, Tjian R (May 1998).
"Functional analysis of the human TAFII250 N-terminal kinase domain" . Mol. Cell . 1 (6): 905–11.
doi :
10.1016/S1097-2765(00)80089-1 .
PMID
9660973 .
^
a
b
c Pointud JC, Mengus G, Brancorsini S, Monaco L, Parvinen M, Sassone-Corsi P, Davidson I (May 2003). "The intracellular localisation of TAF7L, a paralogue of transcription factor TFIID subunit TAF7, is developmentally regulated during male germ-cell differentiation". J. Cell Sci . 116 (Pt 9): 1847–58.
doi :
10.1242/jcs.00391 .
PMID
12665565 .
S2CID
24519687 .
^ Tao Y, Guermah M, Martinez E, Oelgeschläger T, Hasegawa S, Takada R, Yamamoto T, Horikoshi M, Roeder RG (March 1997).
"Specific interactions and potential functions of human TAFII100" . J. Biol. Chem . 272 (10): 6714–21.
doi :
10.1074/jbc.272.10.6714 .
PMID
9045704 .
^ Martinez E, Palhan VB, Tjernberg A, Lymar ES, Gamper AM, Kundu TK, Chait BT, Roeder RG (October 2001).
"Human STAGA complex is a chromatin-acetylating transcription coactivator that interacts with pre-mRNA splicing and DNA damage-binding factors in vivo" . Mol. Cell. Biol . 21 (20): 6782–95.
doi :
10.1128/MCB.21.20.6782-6795.2001 .
PMC
99856 .
PMID
11564863 .
^
a
b Mengus G, May M, Jacq X, Staub A, Tora L, Chambon P, Davidson I (April 1995).
"Cloning and characterization of hTAFII18, hTAFII20 and hTAFII28: three subunits of the human transcription factor TFIID" . EMBO J . 14 (7): 1520–31.
doi :
10.1002/j.1460-2075.1995.tb07138.x .
PMC
398239 .
PMID
7729427 .
^ May M, Mengus G, Lavigne AC, Chambon P, Davidson I (June 1996).
"Human TAF(II28) promotes transcriptional stimulation by activation function 2 of the retinoid X receptors" . EMBO J . 15 (12): 3093–104.
doi :
10.1002/j.1460-2075.1996.tb00672.x .
PMC
450252 .
PMID
8670810 .
^ Hoffmann A, Roeder RG (July 1996).
"Cloning and characterization of human TAF20/15. Multiple interactions suggest a central role in TFIID complex formation" . J. Biol. Chem . 271 (30): 18194–202.
doi :
10.1074/jbc.271.30.18194 .
PMID
8663456 .
^ Hochheimer A, Tjian R (June 2003).
"Diversified transcription initiation complexes expand promoter selectivity and tissue-specific gene expression" . Genes & Development . 17 (11): 1309–20.
doi :
10.1101/gad.1099903 .
PMID
12782648 .
^ Pugh BF (September 2000). "Control of gene expression through regulation of the TATA-binding protein". Gene . 255 (1): 1–14.
doi :
10.1016/s0378-1119(00)00288-2 .
PMID
10974559 .
^ Weaver, Robert Franklin (1 January 2012). Molecular biology . McGraw-Hill.
ISBN
9780073525327 .
OCLC
789601172 .
^ Louder RK, He Y, López-Blanco JR, Fang J, Chacón P, Nogales E (March 2016).
"Structure of promoter-bound TFIID and model of human pre-initiation complex assembly" . Nature . 531 (7596): 604–9.
Bibcode :
2016Natur.531..604L .
doi :
10.1038/nature17394 .
PMC
4856295 .
PMID
27007846 .
^ Davidson I (July 2003). "The genetics of TBP and TBP-related factors". Trends in Biochemical Sciences . 28 (7): 391–8.
doi :
10.1016/S0968-0004(03)00117-8 .
PMID
12878007 .
^ Nikolov DB, Hu SH, Lin J, Gasch A, Hoffmann A, Horikoshi M, Chua NH, Roeder RG, Burley SK (November 1992). "Crystal structure of TFIID TATA-box binding protein". Nature . 360 (6399): 40–6.
Bibcode :
1992Natur.360...40N .
doi :
10.1038/360040a0 .
PMID
1436073 .
S2CID
4307043 .
External links
PDB gallery
1c9b : CRYSTAL STRUCTURE OF A HUMAN TBP CORE DOMAIN-HUMAN TFIIB CORE DOMAIN COMPLEX BOUND TO AN EXTENDED, MODIFIED ADENOVIRAL MAJOR LATE PROMOTER (ADMLP)
1cdw : HUMAN TBP CORE DOMAIN COMPLEXED WITH DNA
1jfi : Crystal Structure of the NC2-TBP-DNA Ternary Complex
1nvp : HUMAN TFIIA/TBP/DNA COMPLEX
1tgh : TATA BINDING PROTEIN (TBP)/DNA COMPLEX
(1) Basic domains
(1.1) Basic
leucine zipper (
bZIP )(1.2) Basic helix-loop-helix (
bHLH )
Group A Group B Group C bHLH-
PAS Group D Group E Group F bHLH-COE
(1.3)
bHLH-ZIP (1.4) NF-1 (1.5) RF-X (1.6) Basic helix-span-helix (bHSH)
(2)
Zinc finger DNA-binding domains
(2.1)
Nuclear receptor (Cys4 )
subfamily 1 subfamily 2 subfamily 3 subfamily 4 subfamily 5 subfamily 6 subfamily 0
(2.2) Other Cys4 (2.3) Cys2 His2 (2.4) Cys6 (2.5) Alternating composition (2.6) WRKY
(4) β-Scaffold factors with minor groove contacts
(0) Other transcription factors