1hoc
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
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| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hoc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hoc OCA], [http://www.ebi.ac.uk/pdbsum/1hoc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hoc RCSB]</span> | ||
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[[Category: histocompatibility antigen]] | [[Category: histocompatibility antigen]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:08:18 2008'' |
Revision as of 18:08, 30 March 2008
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| , resolution 2.4Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE THREE-DIMENSIONAL STRUCTURE OF H-2DB AT 2.4 ANGSTROMS RESOLUTION: IMPLICATIONS FOR ANTIGEN-DETERMINANT SELECTION
Overview
Solution at 2.4 A resolution of the structure of H-2Db with the influenza virus peptide NP366-374 (ASNEN-METM) and comparison with the H-2Kb-VSV (RGY-VYQGL) structure allow description of the molecular details of MHC class I peptide binding interactions for mice of the H-2b haplotype, revealing a strategy that maximizes the repertoire of peptides than can be presented. The H-2Db cleft has a mouse-specific hydrophobic ridge that causes a compensatory arch in the backbone of the peptide, exposing the arch residues to TCR contact and requiring the peptide to be at least 9 residues. This ridge occurs in about 40% of the known murine D and L allelic molecules, classifying them as a structural subgroup.
About this Structure
1HOC is a Protein complex structure of sequences from Influenza a virus and Mus musculus. Full crystallographic information is available from OCA.
Reference
The three-dimensional structure of H-2Db at 2.4 A resolution: implications for antigen-determinant selection., Young AC, Zhang W, Sacchettini JC, Nathenson SG, Cell. 1994 Jan 14;76(1):39-50. PMID:7506996
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