ST staple: Difference between revisions
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Revision as of 15:01, 4 November 2014
Template:Unreviewed 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 alpha-helices and they are usually associated with a slight bend in the helix. Two websites are available for finding and examining Schellman loops in proteins, Motivated Proteins: [motif.gla.ac.uk/motif/index.html] [3]; or PDBeMotif: [www.ebi.ac.uk/pdbe-site/pdbemotif] [4].
References
- ^ Gray, TM; Matthews BW (1984). "Intrahelical hydrogen bonding of serine, threonine and cysteine residues within -helices. Relevance to membrane-bound proteins". Journal of Molecular Biology. 175: 75–82.
- ^ Ballesteros, JA; Deupi X (2000). "Serine and threonine residues bend alpha-helices in the chi(1) 5 g(-) conformation". Biophysical Journal. 79: 2754–2760.
- ^ Leader, DP; Milner-White EJ (2009). "Motivated Proteins: A web application for studying small three-dimensional protein motifs". BMC Bioinformmatics. 10: 60. doi:10.1186/1471-2105-10-60.
{{cite journal}}: CS1 maint: unflagged free DOI (link) - ^ Golovin, A; Henrick K (2008). "MSDmotif: exploring protein sites and motifs". BMC Bioinformatics. 9: 312. doi:10.1186/1471-2105-9-312.
{{cite journal}}: CS1 maint: unflagged free DOI (link)