Accommodating structurally diverse peptides in proteins.
Many peptide-binding proteins must bind numerous ligands that differ in size, sequence and sometimes orientation. A variety of strategies for coping with structurally diverse peptide ligands have been revealed by biochemical and structural studies of proteins with roles in immunity, transport and signal transduction.
Wilkinson
A J
AJ
Department of Chemistry, University of York, Heslington, York YO1 5DD, UK.
D000818:Animals; D001426:Bacterial Proteins; D002147:Calmodulin / Q000737:chemistry; D002352:Carrier Proteins / Q000737:chemistry; D006680:HLA Antigens / Q000737:chemistry; D006649:Histocompatibility Antigens / Q000737:chemistry; D006801:Humans; D008024:Ligands; D008074:Lipoproteins / Q000737:chemistry; D008958:Models, Molecular; D015394:Molecular Structure; D010455:Peptides / Q000737:chemistry*; D011485:Protein Binding; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D018909:src Homology Domains
D001426:Bacterial Proteins; D002147:Calmodulin; D002352:Carrier Proteins; D006680:HLA Antigens; D006649:Histocompatibility Antigens; D008024:Ligands; D008074:Lipoproteins; D010455:Peptides; D011506:Proteins; C046506:oligopeptide-binding protein, bacteria