1t5x: Difference between revisions
New page: left|200px<br /> <applet load="1t5x" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t5x, resolution 2.50Å" /> '''HLA-DR1 in complex ... |
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[[Image:1t5x.gif|left|200px]]<br /> | [[Image:1t5x.gif|left|200px]]<br /><applet load="1t5x" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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caption="1t5x, resolution 2.50Å" /> | caption="1t5x, resolution 2.50Å" /> | ||
'''HLA-DR1 in complex with a synthetic peptide (AAYSDQATPLLLSPR) and the superantigen SEC3-3B2'''<br /> | '''HLA-DR1 in complex with a synthetic peptide (AAYSDQATPLLLSPR) and the superantigen SEC3-3B2'''<br /> | ||
==Overview== | ==Overview== | ||
Peptides bind to class II major histocompatibility complex (MHC) proteins | Peptides bind to class II major histocompatibility complex (MHC) proteins in an extended conformation. Pockets in the peptide binding site spaced to accommodate peptide side chains at the P1, P4, P6, and P9 positions have been previously characterized and help to explain the obtained peptide binding specificity. However, two peptides differing only at P10 have significantly different binding affinities for HLA-DR1. The structure of HLA-DR1 in complex with the tighter binding peptide shows that the peptide binds in the usual polyproline type II conformation, but with the P10 residue accommodated in a shallow pocket at the end of the binding groove. HLA-DR1 variants with polymorphic residues at these positions were produced and found to exhibit different side chain specificity at the P10 position. These results define a new specificity position in HLA-DR proteins. | ||
==About this Structure== | ==About this Structure== | ||
1T5X is a [http://en.wikipedia.org/wiki/Protein_complex 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:// | 1T5X is a [http://en.wikipedia.org/wiki/Protein_complex 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=1T5X OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Staphylococcus aureus]] | [[Category: Staphylococcus aureus]] | ||
[[Category: Anderson, M | [[Category: Anderson, M W.]] | ||
[[Category: Gorski, J.]] | [[Category: Gorski, J.]] | ||
[[Category: Stern, L | [[Category: Stern, L J.]] | ||
[[Category: Strug, I.]] | [[Category: Strug, I.]] | ||
[[Category: Zavala-Ruiz, Z.]] | [[Category: Zavala-Ruiz, Z.]] | ||
[[Category: mhc class ii; major histocompatibiloty complex protein; hla-dr1; superantigen; antigen; peptide]] | [[Category: mhc class ii; major histocompatibiloty complex protein; hla-dr1; superantigen; antigen; peptide]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:10:13 2008'' | ||
Revision as of 16:10, 21 February 2008
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HLA-DR1 in complex with a synthetic peptide (AAYSDQATPLLLSPR) and the superantigen SEC3-3B2
OverviewOverview
Peptides bind to class II major histocompatibility complex (MHC) proteins in an extended conformation. Pockets in the peptide binding site spaced to accommodate peptide side chains at the P1, P4, P6, and P9 positions have been previously characterized and help to explain the obtained peptide binding specificity. However, two peptides differing only at P10 have significantly different binding affinities for HLA-DR1. The structure of HLA-DR1 in complex with the tighter binding peptide shows that the peptide binds in the usual polyproline type II conformation, but with the P10 residue accommodated in a shallow pocket at the end of the binding groove. HLA-DR1 variants with polymorphic residues at these positions were produced and found to exhibit different side chain specificity at the P10 position. These results define a new specificity position in HLA-DR proteins.
About this StructureAbout this Structure
1T5X is a Protein complex structure of sequences from Homo sapiens and Staphylococcus aureus. Full crystallographic information is available from OCA.
ReferenceReference
A polymorphic pocket at the P10 position contributes to peptide binding specificity in class II MHC proteins., Zavala-Ruiz Z, Strug I, Anderson MW, Gorski J, Stern LJ, Chem Biol. 2004 Oct;11(10):1395-402. PMID:15489166
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