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4wco

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Revision as of 07:02, 7 April 2023

Crystal structure of extracellular domain of human lectin-like transcript 1 (LLT1), the ligand for natural killer receptor-P1A

Structural highlights

4wco is a 3 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CLC2D_HUMAN Receptor for KLRB1 that protects target cells against natural killer cell-mediated lysis. Inhibits osteoclast formation. Inhibits bone resorption. Modulates the release of interferon-gamma. Binds high molecular weight sulfated glycosaminoglycans.^[1] ^[2] ^[3]

Publication Abstract from PubMed

Emerging evidence has revealed the pivotal roles of C-type lectin-like receptors (CTLRs) in the regulation of a wide range of immune responses. Human natural killer cell receptor-P1A (NKRP1A) is one of the CTLRs and recognizes another CTLR, lectin-like transcript 1 (LLT1) on target cells to control NK, NKT and Th17 cells. The structural basis for the NKRP1A-LLT1 interaction was limitedly understood. Here, we report the crystal structure of the ectodomain of LLT1. The plausible receptor-binding face of the C-type lectin-like domain is flat, and forms an extended beta-sheet. The residues of this face are relatively conserved with another CTLR, keratinocyte-associated C-type lectin, which binds to the CTLR member, NKp65. A LLT1-NKRP1A complex model, prepared using the crystal structures of LLT1 and the keratinocyte-associated C-type lectin-NKp65 complex, reasonably satisfies the charge consistency and the conformational complementarity to explain a previous mutagenesis study. Furthermore, crystal packing and analytical ultracentrifugation revealed dimer formation, which supports a complex model. Our results provide structural insights for understanding the binding modes and signal transduction mechanisms, which are likely to be conserved in the CTLR family, and for further rational drug design towards regulating the LLT1 function.

Crystal structure of extracellular domain of human lectin-like transcript 1 (LLT1), the ligand for natural killer receptor-P1A.,Kita S, Matsubara H, Kasai Y, Tamaoki T, Okabe Y, Fukuhara H, Kamishikiryo J, Krayukhina E, Uchiyama S, Ose T, Kuroki K, Maenaka K Eur J Immunol. 2015 Jun;45(6):1605-13. doi: 10.1002/eji.201545509. Epub 2015 Apr , 28. PMID:25826155^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Hu YS, Zhou H, Myers D, Quinn JM, Atkins GJ, Ly C, Gange C, Kartsogiannis V, Elliott J, Kostakis P, Zannettino AC, Cromer B, McKinstry WJ, Findlay DM, Gillespie MT, Ng KW. Isolation of a human homolog of osteoclast inhibitory lectin that inhibits the formation and function of osteoclasts. J Bone Miner Res. 2004 Jan;19(1):89-99. PMID:14753741 doi:http://dx.doi.org/10.1359/JBMR.0301215
↑ Mathew PA, Chuang SS, Vaidya SV, Kumaresan PR, Boles KS, Pham HT. The LLT1 receptor induces IFN-gamma production by human natural killer cells. Mol Immunol. 2004 Mar;40(16):1157-63. PMID:15104121
↑ Rosen DB, Bettadapura J, Alsharifi M, Mathew PA, Warren HS, Lanier LL. Cutting edge: lectin-like transcript-1 is a ligand for the inhibitory human NKR-P1A receptor. J Immunol. 2005 Dec 15;175(12):7796-9. PMID:16339513
↑ Kita S, Matsubara H, Kasai Y, Tamaoki T, Okabe Y, Fukuhara H, Kamishikiryo J, Krayukhina E, Uchiyama S, Ose T, Kuroki K, Maenaka K. Crystal structure of extracellular domain of human lectin-like transcript 1 (LLT1), the ligand for natural killer receptor-P1A. Eur J Immunol. 2015 Jun;45(6):1605-13. doi: 10.1002/eji.201545509. Epub 2015 Apr , 28. PMID:25826155 doi:http://dx.doi.org/10.1002/eji.201545509

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4wco"

@@ Line 3: / Line 3: @@
 <StructureSection load='4wco' size='340' side='right'caption='[[4wco]], [[Resolution|resolution]] 2.46&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4wco]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WCO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WCO FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4wco]] is a 3 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=4WCO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WCO FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CLEC2D, CLAX, LLT1, OCIL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4wco FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wco OCA], [https://pdbe.org/4wco PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wco RCSB], [https://www.ebi.ac.uk/pdbsum/4wco PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wco ProSAT]</span></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=4wco FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wco OCA], [http://pdbe.org/4wco PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wco RCSB], [http://www.ebi.ac.uk/pdbsum/4wco PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wco ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CLC2D_HUMAN CLC2D_HUMAN]] Receptor for KLRB1 that protects target cells against natural killer cell-mediated lysis. Inhibits osteoclast formation. Inhibits bone resorption. Modulates the release of interferon-gamma. Binds high molecular weight sulfated glycosaminoglycans.<ref>PMID:14753741</ref> <ref>PMID:15104121</ref> <ref>PMID:16339513</ref>
+[https://www.uniprot.org/uniprot/CLC2D_HUMAN CLC2D_HUMAN] Receptor for KLRB1 that protects target cells against natural killer cell-mediated lysis. Inhibits osteoclast formation. Inhibits bone resorption. Modulates the release of interferon-gamma. Binds high molecular weight sulfated glycosaminoglycans.<ref>PMID:14753741</ref> <ref>PMID:15104121</ref> <ref>PMID:16339513</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 23: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Fukuhara, H]]
+[[Category: Fukuhara H]]
-[[Category: Kamishikiryo, J]]
+[[Category: Kamishikiryo J]]
-[[Category: Kasai, Y]]
+[[Category: Kasai Y]]
-[[Category: Kita, S]]
+[[Category: Kita S]]
-[[Category: Kuroki, K]]
+[[Category: Kuroki K]]
-[[Category: Maenaka, K]]
+[[Category: Maenaka K]]
-[[Category: Matsubara, H]]
+[[Category: Matsubara H]]
-[[Category: Okabe, Y]]
+[[Category: Okabe Y]]
-[[Category: Ose, T]]
+[[Category: Ose T]]
-[[Category: Tamaoki, T]]
+[[Category: Tamaoki T]]
-[[Category: Ectodomain]]
-[[Category: Immune system]]
-[[Category: Immunology]]
-[[Category: Lectin]]
-[[Category: Receptor]]

4wco

From Proteopedia

Revision as of 07:02, 7 April 2023

Crystal structure of extracellular domain of human lectin-like transcript 1 (LLT1), the ligand for natural killer receptor-P1A

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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