1ydp
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1.9A crystal structure of HLA-G
OverviewOverview
HLA-G is a nonclassical major histocompatibility complex class I (MHC-I), molecule that is primarily expressed at the fetal-maternal interface, where it is thought to play a role in protecting the fetus from the, maternal immune response. HLA-G binds a limited repertoire of peptides and, interacts with the inhibitory leukocyte Ig-like receptors LIR-1 and LIR-2, and possibly with certain natural killer cell receptors. To gain further, insights into HLA-G function, we determined the 1.9-A structure of a, monomeric HLA-G complexed to a natural endogenous peptide ligand from, histone H2A (RIIPRHLQL). An extensive network of contacts between the, peptide and the antigen-binding cleft reveal a constrained mode of binding, reminiscent of the nonclassical HLA-E molecule, thereby providing a, structural basis for the limited peptide repertoire of HLA-G. The alpha3, domain of HLA-G, a candidate binding site for the LIR-1 and -2 inhibitory, receptors, is structurally distinct from the alpha3 domains of classical, MHC-I molecules, providing a rationale for the observed affinity, differences for these ligands. The structural data suggest a head-to-tail, mode of dimerization, mediated by an intermolecular disulfide bond, that, is consistent with the observation of HLA-G dimers on the cell surface.
DiseaseDisease
Known diseases associated with this structure: Asthma, susceptibility to OMIM:[142871], Hypoproteinemia, hypercatabolic OMIM:[109700]
About this StructureAbout this Structure
1YDP is a Protein complex structure of sequences from Homo sapiens with CO and CL as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of HLA-G: a nonclassical MHC class I molecule expressed at the fetal-maternal interface., Clements CS, Kjer-Nielsen L, Kostenko L, Hoare HL, Dunstone MA, Moses E, Freed K, Brooks AG, Rossjohn J, McCluskey J, Proc Natl Acad Sci U S A. 2005 Mar 1;102(9):3360-5. Epub 2005 Feb 17. PMID:15718280
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