1g0x: Difference between revisions
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==CRYSTAL STRUCTURE OF THE LIGAND BINDING DOMAIN OF LIR-1 (ILT2)== | ==CRYSTAL STRUCTURE OF THE LIGAND BINDING DOMAIN OF LIR-1 (ILT2)== | ||
<StructureSection load='1g0x' size='340' side='right' caption='[[1g0x]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='1g0x' size='340' side='right' caption='[[1g0x]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1g0x]] is a 1 chain structure | <table><tr><td colspan='2'>[[1g0x]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G0X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1G0X FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g0x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g0x OCA], [http://pdbe.org/1g0x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1g0x RCSB], [http://www.ebi.ac.uk/pdbsum/1g0x PDBsum]</span></td></tr> | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g0x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g0x OCA], [http://pdbe.org/1g0x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1g0x RCSB], [http://www.ebi.ac.uk/pdbsum/1g0x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1g0x ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1g0x ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bjorkman, P J]] | [[Category: Bjorkman, P J]] | ||
[[Category: Chapman, T L]] | [[Category: Chapman, T L]] | ||
Revision as of 13:42, 13 September 2017
CRYSTAL STRUCTURE OF THE LIGAND BINDING DOMAIN OF LIR-1 (ILT2)CRYSTAL STRUCTURE OF THE LIGAND BINDING DOMAIN OF LIR-1 (ILT2)
Structural highlights
Function[LIRB1_HUMAN] Receptor for class I MHC antigens. Recognizes a broad spectrum of HLA-A, HLA-B, HLA-C and HLA-G alleles. Receptor for H301/UL18, a human cytomegalovirus class I MHC homolog. Ligand binding results in inhibitory signals and down-regulation of the immune response. Engagement of LILRB1 present on natural killer cells or T-cells by class I MHC molecules protects the target cells from lysis. Interaction with HLA-B or HLA-E leads to inhibition of the signal triggered by FCER1A and inhibits serotonin release. Inhibits FCGR1A-mediated phosphorylation of cellular proteins and mobilization of intracellular calcium ions.[1] [2] [3] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedLIR-1 is an inhibitory receptor that recognizes class I MHC molecules and the human cytomegalovirus class I homolog UL18. Here, we report the 2.1 A resolution crystal structure of the ligand binding portion of LIR-1 (domains 1 and 2 [D1D2]) and localize the binding region for UL18. LIR-1 D1D2 is composed of two immunoglobulin-like domains arranged at an acute angle to form a bent structure resembling the structures of natural killer inhibitory receptors (KIRs). The LIR-1 binding site comprises a portion of D1 distant from the interdomain hinge region that constitutes the KIR binding site, consistent with differences in LIR-1 and KIR recognition properties and functions. Crystal structure and ligand binding properties of the D1D2 region of the inhibitory receptor LIR-1 (ILT2).,Chapman TL, Heikema AP, West AP Jr, Bjorkman PJ Immunity. 2000 Nov;13(5):727-36. PMID:11114384[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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