2d3v: Difference between revisions

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|PDB= 2d3v |SIZE=350|CAPTION= <scene name='initialview01'>2d3v</scene>, resolution 1.85&Aring;
|PDB= 2d3v |SIZE=350|CAPTION= <scene name='initialview01'>2d3v</scene>, resolution 1.85&Aring;
|SITE=  
|SITE=  
|LIGAND=  
|LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
|ACTIVITY=  
|ACTIVITY=  
|GENE=  
|GENE=  
|DOMAIN=
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2d3v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d3v OCA], [http://www.ebi.ac.uk/pdbsum/2d3v PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2d3v RCSB]</span>
}}
}}


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[[Category: immunoglobulin-like fold]]
[[Category: immunoglobulin-like fold]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:23:01 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:29:58 2008''

Revision as of 02:30, 31 March 2008

File:2d3v.gif


PDB ID 2d3v

Drag the structure with the mouse to rotate
, resolution 1.85Å
Ligands:
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of Leukocyte Ig-like Receptor A5 (LILRA5/LIR9/ILT11)


OverviewOverview

Human leukocyte Ig-like receptor B1 (LILRB1) and B2 (LILRB2) belong to "Group 1" receptors and recognize a broad range of major histocompatibility complex class I molecules (MHCIs). In contrast, "Group 2" receptors show low similarity with LILRB1/B2, and their ligands remain to be identified. To date, the structural and functional characteristics of Group 2 LILRs are poorly understood. Here we report the crystal structure of the extracellular domain of LILRA5, which is an activating Group 2 LILR expressed on monocytes and neutrophils. Unexpectedly, the structure showed large changes in structural conformation and charge distribution in the region corresponding to the MHCI binding site of LILRB1/B2, which are also distinct from killer cell Ig-like receptors and Fc alpha receptors. These changes probably confer the structural hindrance for the MHCI binding, and their key amino acid substitutions are well conserved in Group 2 LILRs. Consistently, the surface plasmon resonance and flow cytometric analyses demonstrated that LILRA5 exhibited no affinities to all tested MHCIs. These results raised the possibility that LILRA5 as well as Group 2 LILRs do not play a role in any MHCI recognition but could possibly bind to non-MHCI ligand(s) on the target cells to provide a novel immune regulation mechanism.

About this StructureAbout this Structure

2D3V is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the human monocyte-activating receptor, "Group 2" leukocyte Ig-like receptor A5 (LILRA5/LIR9/ILT11)., Shiroishi M, Kajikawa M, Kuroki K, Ose T, Kohda D, Maenaka K, J Biol Chem. 2006 Jul 14;281(28):19536-44. Epub 2006 May 3. PMID:16675463

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