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| - | [[Image:2d31.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2d31| PDB=2d31 | SCENE= }} | | {{STRUCTURE_2d31| PDB=2d31 | SCENE= }} |
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| - | '''Crystal structure of disulfide-linked HLA-G dimer'''
| + | ===Crystal structure of disulfide-linked HLA-G dimer=== |
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| - | ==Overview==
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| - | HLA-G is a nonclassical major histocompatibility complex class I (MHCI) molecule, which is expressed in trophoblasts and confers immunological tolerance in the maternal-fetal interface by binding to leukocyte Ig-like receptors (LILRs, also called as LIR/ILT/CD85) and CD8. HLA-G is expressed in disulfide-linked dimer form both in solution and at the cell surface. Interestingly, MHCI dimer formations have been involved in pathogenesis and T cell activation. The structure and receptor binding characteristics of MHCI dimers have never been evaluated. Here we performed binding studies showing that the HLA-G dimer exhibited higher overall affinity to LILRB1/2 than the monomer by significant avidity effects. Furthermore, the cell reporter assay demonstrated that the dimer formation remarkably enhanced the LILRB1-mediated signaling at the cellular level. We further determined the crystal structure of the wild-type dimer of HLA-G with the intermolecular Cys(42)-Cys(42) disulfide bond. This dimer structure showed the oblique configuration to expose two LILR/CD8-binding sites upward from the membrane easily accessible for receptors, providing plausible 1:2 (HLA-G dimer:receptors) complex models. These results indicated that the HLA-G dimer conferred increased avidity in a proper structural orientation to induce efficient LILR signaling, resulting in the dominant immunosuppressive effects. Moreover, structural and functional implications for other MHCI dimers observed in activated T cells and the pathogenic allele, HLA-B27, are discussed.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_16455647}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16455647 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_16455647}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Tsumoto, K.]] | | [[Category: Tsumoto, K.]] |
| | [[Category: Mhc class i]] | | [[Category: Mhc class i]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 23:36:17 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 14:14:35 2008'' |
Revision as of 11:14, 28 July 2008
Template:STRUCTURE 2d31
Crystal structure of disulfide-linked HLA-G dimer
Template:ABSTRACT PUBMED 16455647
About this Structure
2D31 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Efficient leukocyte Ig-like receptor signaling and crystal structure of disulfide-linked HLA-G dimer., Shiroishi M, Kuroki K, Ose T, Rasubala L, Shiratori I, Arase H, Tsumoto K, Kumagai I, Kohda D, Maenaka K, J Biol Chem. 2006 Apr 14;281(15):10439-47. Epub 2006 Feb 2. PMID:16455647
Page seeded by OCA on Mon Jul 28 14:14:35 2008
Categories: Homo sapiens | Protein complex | Arase, H. | Kohda, D. | Kumagai, I. | Kuroki, K. | Maenaka, K. | Ose, T. | Rasubala, L. | Shiratori, I. | Shiroishi, M. | Tsumoto, K. | Mhc class i
