Luxury accommodations: the expanding role of structural plasticity in protein-protein interactions.
The recognition of multiple ligands at a single molecular surface is essential to many biological processes. Conformational flexibility has emerged as a compelling strategy for association at such convergent binding sites. Studies over the past few years have brought about a greater understanding of the role that protein plasticity might play in protein-protein interactions.
Sundberg
E J
EJ
Center for Advanced Research in Biotechnology, University of Maryland, Biotechnology Institute, Rockville, MD 20850, USA.
Mariuzza
R A
RA
D000818:Animals; D000941:Antigens / Q000378:metabolism; D001665:Binding Sites; D016384:Consensus Sequence; D018360:Crystallography, X-Ray; D004921:Erythropoietin / Q000819:agonists / Q000378:metabolism; D015395:Histocompatibility Antigens Class I / Q000378:metabolism; D006801:Humans; D007141:Immunoglobulin Fc Fragments / Q000737:chemistry / Q000378:metabolism; D008024:Ligands; D008958:Models, Molecular; D019151:Peptide Library; D011485:Protein Binding; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000235:genetics / Q000378:metabolism; D011948:Receptors, Antigen, T-Cell / Q000737:chemistry / Q000378:metabolism; D017467:Receptors, Erythropoietin / Q000737:chemistry / Q000378:metabolism; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
D000941:Antigens; D015395:Histocompatibility Antigens Class I; D007141:Immunoglobulin Fc Fragments; D008024:Ligands; D019151:Peptide Library; D011506:Proteins; D011948:Receptors, Antigen, T-Cell; D017467:Receptors, Erythropoietin; D004921:Erythropoietin