1jwu
Crystal Structure of the Complex of the MHC Class II Molecule HLA-DR1 (HA peptide 306-318) with the superantigen SEC3 Variant 3B2
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OverviewOverview
Due to a paucity of studies that synthesize structural, energetic, and, functional analyses of a series of protein complexes representing distinct, stages in an affinity maturation pathway, the biophysical basis for the, molecular evolution of protein-protein interactions is poorly understood., Here, we combine crystal structures and binding-free energies of a series, of variant superantigen (SAG)-major histocompatibility complex (MHC) class, II complexes exhibiting increasingly higher affinity to reveal that this, affinity maturation pathway is controlled largely by two biophysical, factors: shape complementarity and buried hydrophobic surface. These, factors, however, do not contribute equivalently to the affinity, maturation of the interface, as the former dominates the early steps of, the maturation process while the latter is responsible for improved, binding in later steps. Functional assays reveal how affinity maturation, of the SAG-MHC interface corresponds to T cell activation by SAGs.
About this StructureAbout this Structure
1JWU is a Protein complex structure of sequences from Homo sapiens and Staphylococcus aureus. Full crystallographic information is available from OCA.
ReferenceReference
Structural, energetic, and functional analysis of a protein-protein interface at distinct stages of affinity maturation., Sundberg EJ, Andersen PS, Schlievert PM, Karjalainen K, Mariuzza RA, Structure. 2003 Sep;11(9):1151-61. PMID:12962633
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