1ieb

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HISTOCOMPATIBILITY ANTIGENHISTOCOMPATIBILITY ANTIGEN

Structural highlights

1ieb is a 4 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.7Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HA21_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

The high-resolution x-ray crystal structures of the murine major histocompatibility complex (MHC) class II molecule, I-E(k), occupied by either of two antigenic peptides were determined. They reveal the structural basis for the I-E(k) peptide binding motif and suggest general principles for additional alleles. A buried cluster of acidic amino acids in the binding groove predicted to be conserved among all murine I-E and human DR MHC class II molecules suggests how pH may influence MHC binding or exchange of peptides. These structures also complement mutational studies on the importance of individual peptide residues to T cell receptor recognition.

Structures of an MHC class II molecule with covalently bound single peptides.,Fremont DH, Hendrickson WA, Marrack P, Kappler J Science. 1996 May 17;272(5264):1001-4. PMID:8638119[1]

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

See Also

References

  1. Fremont DH, Hendrickson WA, Marrack P, Kappler J. Structures of an MHC class II molecule with covalently bound single peptides. Science. 1996 May 17;272(5264):1001-4. PMID:8638119

1ieb, resolution 2.70Å

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