1ydp: Difference between revisions
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[[Image:1ydp.gif|left|200px]] | [[Image:1ydp.gif|left|200px]] | ||
'''1.9A crystal structure of HLA-G''' | {{Structure | ||
|PDB= 1ydp |SIZE=350|CAPTION= <scene name='initialview01'>1ydp</scene>, resolution 1.9Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene> and <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''1.9A crystal structure of HLA-G''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1YDP is a [ | 1YDP is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YDP OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15718280 15718280] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: immune system]] | [[Category: immune system]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:21:30 2008'' | ||
Revision as of 13:21, 20 March 2008
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| 1ydp, resolution 1.9Å | |||||||||||||
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| Ligands: | CO and CL | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
1.9A crystal structure of HLA-G
Overview
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.
Disease
Known diseases associated with this structure: Asthma, susceptibility to OMIM:[142871], Hypoproteinemia, hypercatabolic OMIM:[109700]
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
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