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The ST pinch: A side chain‐to‐side chain hydrogen‐bonded motif
Author(s) -
Bomar Martha G.,
Raghavender Upadhyayula S.,
Spindel Alexander W. I.,
Kodukula Krishna,
Galande Amit K.
Publication year - 2012
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.24045
Subject(s) - side chain , chemistry , hydrogen bond , linker , residue (chemistry) , structural motif , crystallography , protein structure , stereochemistry , molecule , biochemistry , organic chemistry , computer science , polymer , operating system
The ST Pinch is a 12‐membered hydrogen‐bonded motif (Ser/Thr‐Xaa‐Ser/Thr) involving the side chain oxygen atoms of two Ser/Thr residues. We identified the ST Pinch in 104 proteins in a database containing high‐resolution crystal structures. Conformational analysis of the ST Pinch in these proteins points to specific preferences for the Xaa residue and a high propensity of this residue to adopt positive φ angles. Our results suggest that this motif serves as a linker of secondary structural elements within proteins and is a new addition to the existing list of short hydrogen bond‐stabilized motifs in proteins. Proteins 2012;. © 2012 Wiley Periodicals, Inc.