2d3v
From Proteopedia
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- | [[Image:2d3v.gif|left|200px]] | + | [[Image:2d3v.gif|left|200px]] |
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- | '''Crystal Structure of Leukocyte Ig-like Receptor A5 (LILRA5/LIR9/ILT11)''' | + | {{Structure |
+ | |PDB= 2d3v |SIZE=350|CAPTION= <scene name='initialview01'>2d3v</scene>, resolution 1.85Å | ||
+ | |SITE= | ||
+ | |LIGAND= | ||
+ | |ACTIVITY= | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''Crystal Structure of Leukocyte Ig-like Receptor A5 (LILRA5/LIR9/ILT11)''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 2D3V is a [ | + | 2D3V is a [[Single protein]] structure of sequence 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=2D3V OCA]. |
==Reference== | ==Reference== | ||
- | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16675463 16675463] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: immunoglobulin-like fold]] | [[Category: immunoglobulin-like fold]] | ||
- | ''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 16:23:01 2008'' |
Revision as of 14:23, 20 March 2008
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Coordinates: | save as pdb, mmCIF, xml |
Crystal Structure of Leukocyte Ig-like Receptor A5 (LILRA5/LIR9/ILT11)
Overview
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 Structure
2D3V is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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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