1mhc
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(New page: 200px<br /><applet load="1mhc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mhc, resolution 2.1Å" /> '''MODEL OF MHC CLASS I ...)
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Revision as of 19:17, 20 November 2007
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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 with NAG and FOR as ligands. 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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