2d31: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
Line 1: Line 1:
[[Image:2d31.gif|left|200px]]
{{Seed}}
[[Image:2d31.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2d31|  PDB=2d31  |  SCENE=  }}  
{{STRUCTURE_2d31|  PDB=2d31  |  SCENE=  }}  


'''Crystal structure of disulfide-linked HLA-G dimer'''
===Crystal structure of disulfide-linked HLA-G dimer===




==Overview==
<!--
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.
-->
{{ABSTRACT_PUBMED_16455647}}


==About this Structure==
==About this Structure==
Line 33: Line 37:
[[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

File:2d31.png

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=2d31&oldid=702255"