1mhc
From Proteopedia
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|PDB= 1mhc |SIZE=350|CAPTION= <scene name='initialview01'>1mhc</scene>, resolution 2.1Å | |PDB= 1mhc |SIZE=350|CAPTION= <scene name='initialview01'>1mhc</scene>, resolution 2.1Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=FOR:FORMYL+GROUP'>FOR</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= H2-M3 B2M ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | |GENE= H2-M3 B2M ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mhc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mhc OCA], [http://www.ebi.ac.uk/pdbsum/1mhc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mhc RCSB]</span> | ||
}} | }} | ||
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[[Category: Lindahl, K Fischer.]] | [[Category: Lindahl, K Fischer.]] | ||
[[Category: Wang, C R.]] | [[Category: Wang, C R.]] | ||
| - | [[Category: FOR]] | ||
| - | [[Category: NAG]] | ||
[[Category: histocompatibility antigen/peptide]] | [[Category: histocompatibility antigen/peptide]] | ||
| - | ''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 22:16:01 2008'' |
Revision as of 19:16, 30 March 2008
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| , resolution 2.1Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | H2-M3 B2M (Mus musculus) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
MODEL OF MHC CLASS I H2-M3 WITH NONAPEPTIDE FROM RAT ND1 REFINED AT 2.3 ANGSTROMS RESOLUTION
Overview
H2-M3 is a class Ib MHC molecule of the mouse with a 10(4)-fold preference for binding N-formylated peptides. To elucidate the basis of this unusual specificity, we expressed and crystallized a soluble form of M3 with a formylated nonamer peptide, fMYFINILTL, and determined the structure by X-ray crystallography. M3, refined at 2.1 A resolution, resembles class la MHC molecules in its overall structure, but differs in the peptide-binding groove. The A pocket, which usually accommodates the free N-terminus of a bound peptide, is closed, and the peptide is shifted one residue, such that the P1 side chain is lodged in the B pocket. The formyl group is coordinated by His-9 and a bound water on the floor of the groove.
About this Structure
1MHC is a Protein complex structure of sequences from Mus musculus and Rattus rattus. Full crystallographic information is available from OCA.
Reference
Nonclassical binding of formylated peptide in crystal structure of the MHC class Ib molecule H2-M3., Wang CR, Castano AR, Peterson PA, Slaughter C, Lindahl KF, Deisenhofer J, Cell. 1995 Aug 25;82(4):655-64. PMID:7664344
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