1g0x

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[[Image:1g0x.gif|left|200px]]
 
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{{Structure
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==CRYSTAL STRUCTURE OF THE LIGAND BINDING DOMAIN OF LIR-1 (ILT2)==
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|PDB= 1g0x |SIZE=350|CAPTION= <scene name='initialview01'>1g0x</scene>, resolution 2.10&Aring;
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<StructureSection load='1g0x' size='340' side='right'caption='[[1g0x]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1g0x]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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 [https://proteopedia.org/fgij/fg.htm?mol=1G0X FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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|GENE=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1g0x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g0x OCA], [https://pdbe.org/1g0x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g0x RCSB], [https://www.ebi.ac.uk/pdbsum/1g0x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g0x ProSAT]</span></td></tr>
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}}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/LIRB1_HUMAN 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.<ref>PMID:9285411</ref> <ref>PMID:9842885</ref> <ref>PMID:11907092</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g0/1g0x_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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LIR-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.
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'''CRYSTAL STRUCTURE OF THE LIGAND BINDING DOMAIN OF LIR-1 (ILT2)'''
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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<ref>PMID:11114384</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1g0x" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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LIR-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.
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*[[Leukocyte immunoglobulin-like receptor|Leukocyte immunoglobulin-like receptor]]
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== References ==
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==About this Structure==
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<references/>
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1G0X 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=1G0X OCA].
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__TOC__
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</StructureSection>
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/11114384 11114384]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Bjorkman, P J.]]
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[[Category: Bjorkman PJ]]
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[[Category: Chapman, T L.]]
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[[Category: Chapman TL]]
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[[Category: Heikema, A P.]]
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[[Category: Heikema AP]]
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[[Category: Jr., A P.West.]]
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[[Category: West Jr AP]]
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[[Category: 3-10 helix]]
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[[Category: immunoglobulin fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:16:38 2008''
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Current revision

CRYSTAL STRUCTURE OF THE LIGAND BINDING DOMAIN OF LIR-1 (ILT2)

PDB ID 1g0x

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