ST staple
The ST staple is a common four- or five-amino acid residue motif in proteins and polypeptides with serine or threonine as the C-terminal residue.[1][2] It is characterized by a single hydrogen bond between the hydroxyl group of the serine or threonine (at residue i + 3 or i + 4) and the main chain carbonyl group of residue i. Motifs are of two types, depending whether the motif has 4 or 5 residues. Most ST staples occur in conjunction with an alpha helix, and are usually associated with a slight bend in the helix. Two websites are available for finding and examining ST staples in proteins: Motivated Proteins[3] and PDBeMotif.[4]
References
[edit]- ^ Gray, TM; Matthews BW (1984). "Intrahelical hydrogen bonding of serine, threonine and cysteine residues within α-helices. Relevance to membrane-bound proteins". Journal of Molecular Biology. 175 (1): 75–82. doi:10.1016/0022-2836(84)90446-7. PMID 6427470.
- ^ Ballesteros, JA; Deupi X (2000). "Serine and threonine residues bend alpha-helices in the chi(1) 5 g(-) conformation". Biophysical Journal. 79 (5): 2754–2760. Bibcode:2000BpJ....79.2754B. doi:10.1016/S0006-3495(00)76514-3. PMC 1301156. PMID 11053148.
- ^ Leader, DP; Milner-White EJ (2009). "Motivated Proteins: A web application for studying small three-dimensional protein motifs". BMC Bioinformatics. 10 (1): 60. doi:10.1186/1471-2105-10-60. PMC 2651126. PMID 19210785.
- ^ Golovin, A; Henrick K (2008). "MSDmotif: exploring protein sites and motifs". BMC Bioinformatics. 9 (1): 312. doi:10.1186/1471-2105-9-312. PMC 2491636. PMID 18637174.