3ueh: Difference between revisions

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== Function ==
== 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>  
[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>  
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== Publication Abstract from PubMed ==
Survivin, a subunit of the Chromosome Passenger Complex, binds the N-terminal tail of histone H3, which is phosphorylated on T3 by Haspin kinase, and localizes the complex to the inner centromeres. We used X-ray crystallography to determine the residues of Survivin that are important in binding phosphomodified histone H3. Mutation of amino acids that interact with the histone N-terminus lowered in vitro tail binding affinity and reduced CPC recruitment to the inner centromere in cells, validating our solved structures. Phylogenetic analysis shows that non-mammalian vertebrates have two Survivin paralogs, which we name Class A and B. A distinguishing feature of these paralogs is H to R change in an amino acid that interacts with the histone T3 phosphate. The binding to histone tails of the human Class A paralog, which has a histidine at this position, is sensitive to changes around physiological pH, while Xenopus Survivin Class B is less so. Our data demonstrate that Survivin paralogs have different characteristics of phosphospecific binding to threonine-3 of histone H3, providing new insight into the biology of the inner centromere.
Molecular basis for phosphospecific recognition of histone H3 tails by Survivin paralogs at inner centromeres.,Niedzialkowska E, Wang F, Porebski PJ, Minor W, Higgins JM, Stukenberg PT Mol Biol Cell. 2012 Feb 22. PMID:22357620<ref>PMID:22357620</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 3ueh" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==

Latest revision as of 16:55, 14 March 2024

Crystal structure of human Survivin H80A mutantCrystal structure of human Survivin H80A mutant

Structural highlights

3ueh is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.6Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.[1] [2] [3] [4] [5] [6] [7] [8]

See Also

References

  1. ↑ Mahotka C, Wenzel M, Springer E, Gabbert HE, Gerharz CD. Survivin-deltaEx3 and survivin-2B: two novel splice variants of the apoptosis inhibitor survivin with different antiapoptotic properties. Cancer Res. 1999 Dec 15;59(24):6097-102. PMID:10626797
  2. ↑ Li F, Ambrosini G, Chu EY, Plescia J, Tognin S, Marchisio PC, Altieri DC. Control of apoptosis and mitotic spindle checkpoint by survivin. Nature. 1998 Dec 10;396(6711):580-4. PMID:9859993 doi:10.1038/25141
  3. ↑ Marusawa H, Matsuzawa S, Welsh K, Zou H, Armstrong R, Tamm I, Reed JC. HBXIP functions as a cofactor of survivin in apoptosis suppression. EMBO J. 2003 Jun 2;22(11):2729-40. PMID:12773388 doi:10.1093/emboj/cdg263
  4. ↑ Vong QP, Cao K, Li HY, Iglesias PA, Zheng Y. Chromosome alignment and segregation regulated by ubiquitination of survivin. Science. 2005 Dec 2;310(5753):1499-504. PMID:16322459 doi:10.1126/science.1120160
  5. ↑ Noton EA, Colnaghi R, Tate S, Starck C, Carvalho A, Ko Ferrigno P, Wheatley SP. Molecular analysis of survivin isoforms: evidence that alternatively spliced variants do not play a role in mitosis. J Biol Chem. 2006 Jan 13;281(2):1286-95. Epub 2005 Nov 16. PMID:16291752 doi:M508773200
  6. ↑ Xia F, Canovas PM, Guadagno TM, Altieri DC. A survivin-ran complex regulates spindle formation in tumor cells. Mol Cell Biol. 2008 Sep;28(17):5299-311. Epub 2008 Jun 30. PMID:18591255 doi:10.1128/MCB.02039-07
  7. ↑ Wang H, Holloway MP, Ma L, Cooper ZA, Riolo M, Samkari A, Elenitoba-Johnson KS, Chin YE, Altura RA. Acetylation directs survivin nuclear localization to repress STAT3 oncogenic activity. J Biol Chem. 2010 Nov 12;285(46):36129-37. doi: 10.1074/jbc.M110.152777. Epub, 2010 Sep 8. PMID:20826784 doi:10.1074/jbc.M110.152777
  8. ↑ Pavlyukov MS, Antipova NV, Balashova MV, Vinogradova TV, Kopantzev EP, Shakhparonov MI. Survivin monomer plays an essential role in apoptosis regulation. J Biol Chem. 2011 Jul 1;286(26):23296-307. doi: 10.1074/jbc.M111.237586. Epub, 2011 May 2. PMID:21536684 doi:10.1074/jbc.M111.237586

3ueh, resolution 2.60Å

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