3m9z
From Proteopedia
(Difference between revisions)
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<StructureSection load='3m9z' size='340' side='right' caption='[[3m9z]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='3m9z' size='340' side='right' caption='[[3m9z]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3m9z]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[3m9z]] is a 1 chain structure with sequence from [http://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=3M9Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3M9Z FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1e87|1e87]], [[1egg|1egg]], [[1ixx|1ixx]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1e87|1e87]], [[1egg|1egg]], [[1ixx|1ixx]]</td></tr> | ||
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Klrb1a, Ly55, Ly55a, Nkrp1a ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Klrb1a, Ly55, Ly55a, Nkrp1a ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=3m9z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m9z OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3m9z RCSB], [http://www.ebi.ac.uk/pdbsum/3m9z PDBsum]</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=3m9z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m9z OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3m9z RCSB], [http://www.ebi.ac.uk/pdbsum/3m9z PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/KLRBA_MOUSE KLRBA_MOUSE]] Plays a stimulatory role on natural killer (NK) cell cytotoxicity.<ref>PMID:16751398</ref> | [[http://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> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Lk3 transgenic mice]] |
[[Category: Bezouska, K]] | [[Category: Bezouska, K]] | ||
[[Category: Dohnalek, J]] | [[Category: Dohnalek, J]] | ||
Revision as of 07:13, 18 February 2015
Crystal Structure of extracellular domain of mouse NKR-P1A
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