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| {{STRUCTURE_1ydp| PDB=1ydp | SCENE= }} | | {{STRUCTURE_1ydp| PDB=1ydp | SCENE= }} |
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- | '''1.9A crystal structure of HLA-G'''
| + | ===1.9A crystal structure of HLA-G=== |
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- | ==Overview==
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- | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15718280}}, adds the Publication Abstract to the page |
| + | (as it appears on PubMed at http://www.pubmed.gov), where 15718280 is the PubMed ID number. |
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| + | {{ABSTRACT_PUBMED_15718280}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Rossjohn, J.]] | | [[Category: Rossjohn, J.]] |
| [[Category: Immune system]] | | [[Category: Immune system]] |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:11:48 2008'' | + | |
| + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 21:35:46 2008'' |
Revision as of 18:35, 27 July 2008
Template:STRUCTURE 1ydp
1.9A crystal structure of HLA-G
Template:ABSTRACT PUBMED 15718280
About this Structure
1YDP is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Sun Jul 27 21:35:46 2008
Categories: Homo sapiens | Protein complex | Brooks, A G. | Clements, C S. | Dunstone, M A. | Freed, K. | Hoare, H L. | Kjer-nielsen, L. | Kostenko, L. | Mccluskey, J. | Moses, E. | Rossjohn, J. | Immune system