3m9z: Difference between revisions
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New page: '''Unreleased structure''' The entry 3m9z is ON HOLD Authors: Kolenko, P., Rozbesky, D., Bezouska, K., Hasek, J., Dohnalek, J. Description: Crystal Structure of extracellular domain of... |
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The | ==Crystal Structure of extracellular domain of mouse NKR-P1A== | ||
<StructureSection load='3m9z' size='340' side='right'caption='[[3m9z]], [[Resolution|resolution]] 1.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3m9z]] is a 1 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=3M9Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3M9Z FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=3m9z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m9z OCA], [https://pdbe.org/3m9z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3m9z RCSB], [https://www.ebi.ac.uk/pdbsum/3m9z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3m9z ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/KLRBA_MOUSE KLRBA_MOUSE] Plays a stimulatory role on natural killer (NK) cell cytotoxicity.<ref>PMID:16751398</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Receptors belonging to NKR-P1 family and their specific Clr ligands form an alternative missing self recognition system critical in immunity against tumors and viruses, elimination of tumor cells subjected to genotoxic stress, activation of T cell dependent immune response, and hypertension. The three-dimensional structure of the extracellular domain of the mouse natural killer (NK) cell receptor mNKR-P1Aex has been determined by X-ray diffraction. The core of the C-type lectin domain (CTLD) is homologous to the other CTLD receptors whereas one quarter of the domain forms an extended loop interacting tightly with a neighboring loop in the crystal. This domain swapping mechanism results in a compact interaction interface. A second dimerization interface resembles the known arrangement of other CTLD NK receptors. A functional dimeric form of the receptor is suggested, with the loop, evolutionarily conserved within this family, proposed to participate in interactions with ligands. | |||
Molecular architecture of mouse activating NKR-P1 receptors.,Kolenko P, Rozbesky D, Vanek O, Kopecky V Jr, Hofbauerova K, Novak P, Pompach P, Hasek J, Skalova T, Bezouska K, Dohnalek J J Struct Biol. 2011 Sep;175(3):434-41. doi: 10.1016/j.jsb.2011.05.001. Epub 2011 , May 12. PMID:21600988<ref>PMID:21600988</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3m9z" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mus musculus]] | |||
[[Category: Bezouska K]] | |||
[[Category: Dohnalek J]] | |||
[[Category: Hasek J]] | |||
[[Category: Kolenko P]] | |||
[[Category: Rozbesky D]] | |||
Latest revision as of 08:50, 6 September 2023
Crystal Structure of extracellular domain of mouse NKR-P1A
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