1jwu: Difference between revisions

Revision as of 17:38, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1jwu.png

Template:STRUCTURE 1jwu

Crystal Structure of the Complex of the MHC Class II Molecule HLA-DR1 (HA peptide 306-318) with the superantigen SEC3 Variant 3B2Crystal Structure of the Complex of the MHC Class II Molecule HLA-DR1 (HA peptide 306-318) with the superantigen SEC3 Variant 3B2

Template:ABSTRACT PUBMED 12962633

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

Page seeded by OCA on Sun Jul 27 17:38:06 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Crystal Structure of the Complex of the MHC Class II Molecule HLA-DR1 (HA peptide 306-318) with the superantigen SEC3 Variant 3B2'''
+===Crystal Structure of the Complex of the MHC Class II Molecule HLA-DR1 (HA peptide 306-318) with the superantigen SEC3 Variant 3B2===
-==Overview==
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-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_12962633}}, adds the Publication Abstract to the page
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 [[Category: Hla-dr1 beta subunit]]
 [[Category: Mutation]]
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