The importance of extended conformations and, in particular, the PII conformation for the molecular recognition of peptides.
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 PII conformation (left-handed extended polyproline II) in free solution.
Siligardi
G
G
Department of Chemistry, Birkbeck College, University of London, United Kingdom.
Drake
A F
AF
D000595:Amino Acid Sequence; D000936:Antigen-Antibody Complex / Q000737:chemistry; D001665:Binding Sites; D002942:Circular Dichroism; D004247:DNA / Q000737:chemistry / Q000378:metabolism; D000939:Epitopes / Q000737:chemistry / Q000276:immunology; D008024:Ligands; D008969:Molecular Sequence Data; D011480:Protease Inhibitors / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding; D011487:Protein Conformation; D017433:Protein Structure, Secondary
D000936:Antigen-Antibody Complex; D000939:Epitopes; D008024:Ligands; D011480:Protease Inhibitors; D004247:DNA