2rax
From Proteopedia
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- | [[Image:2rax.png|left|200px]] | ||
- | + | ==Crystal structure of Borealin (20-78) bound to Survivin (1-120)== | |
+ | <StructureSection load='2rax' size='340' side='right'caption='[[2rax]], [[Resolution|resolution]] 3.30Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[2rax]] is a 6 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=2RAX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RAX 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]] 3.3Å</td></tr> | ||
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=2rax FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rax OCA], [https://pdbe.org/2rax PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rax RCSB], [https://www.ebi.ac.uk/pdbsum/2rax PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rax ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/BIRC5_HUMAN BIRC5_HUMAN] Multitasking protein that has dual roles in promoting cell proliferation and preventing apoptosis. Component of a chromosome passage protein complex (CPC) which is essential for chromosome alignment and segregation during mitosis and cytokinesis. Acts as an important regulator of the localization of this complex; directs CPC movement to different locations from the inner centromere during prometaphase to midbody during cytokinesis and participates in the organization of the center spindle by associating with polymerized microtubules. The complex with RAN plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules. May counteract a default induction of apoptosis in G2/M phase. The acetylated form represses STAT3 transactivation of target gene promoters. May play a role in neoplasia. Inhibitor of CASP3 and CASP7. Isoform 2 and isoform 3 do not appear to play vital roles in mitosis. Isoform 3 shows a marked reduction in its anti-apoptotic effects when compared with the displayed wild-type isoform.<ref>PMID:10626797</ref> <ref>PMID:9859993</ref> <ref>PMID:12773388</ref> <ref>PMID:16322459</ref> <ref>PMID:16291752</ref> <ref>PMID:18591255</ref> <ref>PMID:20826784</ref> <ref>PMID:21536684</ref> | ||
+ | == Evolutionary Conservation == | ||
+ | [[Image:Consurf_key_small.gif|200px|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ra/2rax_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </jmolCheckbox> | ||
+ | </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=2rax ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
- | == | + | ==See Also== |
- | + | *[[Borealin|Borealin]] | |
- | + | *[[Survivin|Survivin]] | |
- | + | == References == | |
- | + | <references/> | |
- | [[ | + | __TOC__ |
- | + | </StructureSection> | |
- | == | + | |
- | < | + | |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
- | [[Category: | + | [[Category: Large Structures]] |
- | [[Category: | + | [[Category: Hymowitz SG]] |
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Current revision
Crystal structure of Borealin (20-78) bound to Survivin (1-120)
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