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...

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Bibliographic Details
Published inStructure Vol. 8; no. 7; pp. R137 - R142
Main Authors Sundberg, Eric J, Mariuzza, Roy A
Format Book Review Journal Article
LanguageEnglish
Published United States Elsevier Inc 15.07.2000
Subjects
Animals
Antigens - metabolism
Binding Sites
Consensus Sequence
Crystallography, X-Ray
Erythropoietin - agonists
Erythropoietin - metabolism
Histocompatibility Antigens Class I - metabolism
Humans
Immunoglobulin Fc Fragments - chemistry
Immunoglobulin Fc Fragments - metabolism
Ligands
Models, Molecular
Peptide Library
Protein Binding
Protein Conformation
Protein Structure, Tertiary
Proteins - genetics
Proteins - metabolism
Receptors, Antigen, T-Cell - chemistry
Receptors, Antigen, T-Cell - metabolism
Receptors, Erythropoietin - chemistry
Receptors, Erythropoietin - metabolism
Structure-Activity Relationship
Substrate Specificity
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Summary: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.
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ISSN:0969-2126
1878-4186
DOI:10.1016/S0969-2126(00)00167-2