3rs1

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Revision as of 12:35, 14 March 2024

Mouse C-type lectin-related protein Clrg

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Retrieved from "http://52.214.119.220/wiki/index.php/3rs1"

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 <StructureSection load='3rs1' size='340' side='right'caption='[[3rs1]], [[Resolution|resolution]] 1.94&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3rs1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RS1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RS1 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3rs1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RS1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RS1 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.94&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Clec2i, Clrg, Dcl1, Ocilrp2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></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=3rs1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rs1 OCA], [https://pdbe.org/3rs1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rs1 RCSB], [https://www.ebi.ac.uk/pdbsum/3rs1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rs1 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/CLC2I_MOUSE CLC2I_MOUSE]] Inhibits osteoclast formation. Receptor for KLRB1F. Enhances T-cell activation. Plays a role in splenocyte activation, T-cell responses and IL-2 production.<ref>PMID:12374791</ref> <ref>PMID:15963483</ref>
+[https://www.uniprot.org/uniprot/CLC2I_MOUSE CLC2I_MOUSE] Inhibits osteoclast formation. Receptor for KLRB1F. Enhances T-cell activation. Plays a role in splenocyte activation, T-cell responses and IL-2 production.<ref>PMID:12374791</ref> <ref>PMID:15963483</ref>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Interactions between C-type lectin-like NK cell receptors and their protein ligands form one of the key recognition mechanisms of the innate immune system that is involved in the elimination of cells that have been malignantly transformed, virally infected, or stressed by chemotherapy or other factors. We determined an x-ray structure for the extracellular domain of mouse C-type lectin related (Clr) protein g, a ligand for the activation receptor NKR-P1F. Clr-g forms dimers in the crystal structure resembling those of human CD69. This newly reported structure, together with the previously determined structure of mouse receptor NKR-P1A, allowed the modeling and calculations of electrostatic profiles for other closely related receptors and ligands. Despite the high similarity among Clr-g, Clr-b, and human CD69, these molecules have fundamentally different electrostatics, with distinct polarization of Clr-g. The electrostatic profile of NKR-P1F is complementary to that of Clr-g, which suggests a plausible interaction mechanism based on contacts between surface sites of opposite potential.
-Mouse Clr-g, a Ligand for NK Cell Activation Receptor NKR-P1F: Crystal Structure and Biophysical Properties.,Skalova T, Kotynkova K, Duskova J, Hasek J, Kovai T, Kolenko P, Novak P, Man P, Hanc P, Vanek O, Bezouska K, Dohnalek J J Immunol. 2012 Nov 15;189(10):4881-9. doi: 10.4049/jimmunol.1200880. Epub 2012, Oct 15. PMID:23071282<ref>PMID:23071282</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3rs1" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
@@ Line 24: / Line 15: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Lk3 transgenic mice]]
+[[Category: Mus musculus]]
-[[Category: Bezouska, K]]
+[[Category: Bezouska K]]
-[[Category: Dohnalek, J]]
+[[Category: Dohnalek J]]
-[[Category: Duskova, J]]
+[[Category: Duskova J]]
-[[Category: Hasek, J]]
+[[Category: Hasek J]]
-[[Category: Kotynkova, K]]
+[[Category: Kotynkova K]]
-[[Category: Koval, T]]
+[[Category: Koval T]]
-[[Category: Skalova, T]]
+[[Category: Skalova T]]
-[[Category: Stepankova, A]]
+[[Category: Stepankova A]]
-[[Category: Vanek, O]]
+[[Category: Vanek O]]
-[[Category: C-type lectin-like]]
-[[Category: Immune system]]
-[[Category: Ligand of nk receptor]]
-[[Category: Natural killer cell receptor]]
-[[Category: Surface of activated t lymphocyte]]

3rs1

From Proteopedia

Revision as of 12:35, 14 March 2024

Mouse C-type lectin-related protein Clrg

Structural highlights

Function

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