1mhc

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MODEL OF MHC CLASS I H2-M3 WITH NONAPEPTIDE FROM RAT ND1 REFINED AT 2.3 ANGSTROMS RESOLUTION

Structural highlights

1mhc is a 6 chain structure with sequence from Mus musculus and Rattus rattus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.1Å
Ligands:FME, NAG
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q31093_MOUSE

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Citations
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See Also

References

  1. Wang CR, Castano AR, Peterson PA, Slaughter C, Lindahl KF, Deisenhofer J. Nonclassical binding of formylated peptide in crystal structure of the MHC class Ib molecule H2-M3. Cell. 1995 Aug 25;82(4):655-64. PMID:7664344

Contents


PDB ID 1mhc

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