The ST turn is a structural feature in
proteins and
polypeptides.[1] Each consists of three
amino acid residues (labeled i, i + 1 and i + 2) in which residue i is a
serine (S) or
threonine (T) that forms a
hydrogen bond from its sidechain oxygen group to the mainchain NH group of residue i + 2.[2][3]
Similar
motifs occur with
aspartate or
asparagine as residue i, called
asx turn. Four types of
asx turn and ST turn can be distinguished: types I, I’, II and II’. These categories correspond (via sidechain-mainchain mimicry of residue i) to those of the more abundant hydrogen-bonded
beta turns, which have four residues and a hydrogen bond between the CO of residue i and the NH of residue i + 3. Regarding their occurrence in proteins, they differ in that type I is the commonest of the four
beta turns while type II’ is the commonest of the ST and asx turns.
Asx and ST turns both occur frequently at the
N-termini of
α-helices,[4][5][6][7] as part of
asx motifs or
ST motifs, with the asx, serine or threonine as the
N cap residue. They are thus often regarded as helix capping features.
Evidence for a functionally relevant ST turn is provided in the CDR3 region of the T-cell receptor (B chain, V domain) [8]
A proportion of ST turns are accompanied by a mainchain-mainchain hydrogen bond that qualifies them as
ST motifs.