Structural highlights
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
- ↑ 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
