1jwu: Difference between revisions
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[[Image:1jwu.gif|left|200px]] | [[Image:1jwu.gif|left|200px]] | ||
'''Crystal Structure of the Complex of the MHC Class II Molecule HLA-DR1 (HA peptide 306-318) with the superantigen SEC3 Variant 3B2''' | {{Structure | ||
|PDB= 1jwu |SIZE=350|CAPTION= <scene name='initialview01'>1jwu</scene>, resolution 2.30Å | |||
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|LIGAND= | |||
|ACTIVITY= | |||
|GENE= | |||
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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''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1JWU is a [ | 1JWU is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JWU OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12962633 12962633] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: mutation]] | [[Category: mutation]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:09:33 2008'' | ||
Revision as of 13:09, 20 March 2008
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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
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
Page seeded by OCA on Thu Mar 20 12:09:33 2008