title: The ST Pinch: A side chain-to-side chain hydrogen-bonded motif.
abstract: 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.
authors.affiliation: Center for Advanced Drug Research, SRI International, Harrisonburg, Virginia 22802, USA.
authors.forename: Martha G
authors.initials: MG
authors.lastname: Bomar
authors.forename: Upadhyayula S
authors.initials: US
authors.lastname: Raghavender
authors.forename: Alexander W I
authors.initials: AW
authors.lastname: Spindel
authors.forename: Krishna
authors.initials: K
authors.lastname: Kodukula
authors.forename: Amit K
authors.initials: AK
authors.lastname: Galande
mesh_terms: D020816:Amino Acid Motifs; D000596:Amino Acids / Q000737:chemistry*; D030562:Databases, Protein; D006860:Hydrogen Bonding; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation
chemical_list: D000596:Amino Acids; D010455:Peptides