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The importance of extended conformations and, in particular, the P II conformation for the molecular recognition of peptides
Author(s) -
Siligardi Giuliano,
Drake Alex F.
Publication year - 1995
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360370406
Subject(s) - polyproline helix , chemistry , peptide , epitope , nuclear overhauser effect , major histocompatibility complex , stereochemistry , molecular recognition , nuclear magnetic resonance spectroscopy , ligand (biochemistry) , two dimensional nuclear magnetic resonance spectroscopy , crystallography , biochemistry , antibody , molecule , receptor , genetics , organic chemistry , biology , gene
Crystallographic, isotopic labeling nmr and transferred nuclear Overhauser effect studies have highlighted the extended conformation as a very important element of secondary structure at the binding site of many peptide/protein complexes including peptide inhibitors–enzymes, B‐cell epitopes–antibodies, and T‐cell epitopes–major histocompatibility complex (MHC) of class I and II complexes. This paper discusses the peptide ligand conformation consequences of these findings particularly in view of the identification of the P II conformation (left‐handed extended polyproline II) in free solution. © 1994 John Wiley & Sons, Inc.