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1ydp
From Proteopedia
(New page: 200px<br /> <applet load="1ydp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ydp, resolution 1.9Å" /> '''1.9A crystal structu...) |
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| - | [[Image:1ydp.gif|left|200px]]<br /> | + | [[Image:1ydp.gif|left|200px]]<br /><applet load="1ydp" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1ydp" size=" | + | |
caption="1ydp, resolution 1.9Å" /> | caption="1ydp, resolution 1.9Å" /> | ||
'''1.9A crystal structure of HLA-G'''<br /> | '''1.9A crystal structure of HLA-G'''<br /> | ||
==Overview== | ==Overview== | ||
| - | HLA-G is a nonclassical major histocompatibility complex class I (MHC-I) | + | 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== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1YDP is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CO and CL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1YDP is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CO:'>CO</scene> and <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YDP OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Brooks, A | + | [[Category: Brooks, A G.]] |
| - | [[Category: Clements, C | + | [[Category: Clements, C S.]] |
| - | [[Category: Dunstone, M | + | [[Category: Dunstone, M A.]] |
[[Category: Freed, K.]] | [[Category: Freed, K.]] | ||
| - | [[Category: Hoare, H | + | [[Category: Hoare, H L.]] |
[[Category: Kjer-nielsen, L.]] | [[Category: Kjer-nielsen, L.]] | ||
[[Category: Kostenko, L.]] | [[Category: Kostenko, L.]] | ||
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[[Category: immune system]] | [[Category: immune system]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:04:19 2008'' |
Revision as of 14:04, 21 February 2008
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1.9A crystal structure of HLA-G
Contents |
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 with and as ligands. 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 Thu Feb 21 16:04:19 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. | CL | CO | Immune system
