Abstract
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.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Animals
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Antigens / metabolism
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Binding Sites*
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Consensus Sequence
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Crystallography, X-Ray
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Erythropoietin / agonists
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Erythropoietin / metabolism
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Histocompatibility Antigens Class I / metabolism
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Humans
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Immunoglobulin Fc Fragments / chemistry
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Immunoglobulin Fc Fragments / metabolism
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Ligands
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Models, Molecular
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Peptide Library
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Protein Binding*
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Protein Conformation
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Protein Structure, Tertiary
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Proteins / genetics
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Proteins / metabolism
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Receptors, Antigen, T-Cell / chemistry
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Receptors, Antigen, T-Cell / metabolism
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Receptors, Erythropoietin / chemistry
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Receptors, Erythropoietin / metabolism
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Structure-Activity Relationship
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Substrate Specificity
Substances
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Antigens
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Histocompatibility Antigens Class I
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Immunoglobulin Fc Fragments
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Ligands
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Peptide Library
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Proteins
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Receptors, Antigen, T-Cell
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Receptors, Erythropoietin
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Erythropoietin