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4a0j

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Revision as of 17:43, 4 August 2016

CRYSTAL STRUCTURE OF SURVIVIN BOUND TO THE PHOSPHORYLATED N-TERMINAL TAIL OF HISTONE H3

Structural highlights

4a0j is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Related:	1f3h, 1e31, 1xox, 4a0i
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]

Publication Abstract from PubMed

Localization of the chromosomal passenger complex (CPC) at centromeres during early mitosis is essential for accurate chromosome segregation and is dependent on the phosphorylation of histone H3. We report the 2.7 A resolution structure of the CPC subunit Survivin bound to the N-terminal tail of histone H3 carrying the Thr3 phosphorylation mark (Thr3ph). The BIR domain of Survivin recognizes the Ala1-Arg2-Thr3ph-Lys4 sequence, decoding the modification state and the free N terminus of histone H3 by a strategy similar to that used by PHD fingers. The structural analysis permitted the identification of putative Survivin-binding epitopes in other mitotic proteins, including human Shugoshin 1. Using biophysical and structural data, we show that a phospho-mimic N-terminal sequence such as that of hSgo1 (Ala1-Lys2-Glu3-Arg4) contains the specificity determinants to bind Survivin. Our findings suggest that the CPC engages in mutually exclusive interactions with other constituents of the mitotic machinery and a histone mark in chromatin.

Structural Basis for the Recognition of Phosphorylated Histone H3 by the Survivin Subunit of the Chromosomal Passenger Complex.,Jeyaprakash AA, Basquin C, Jayachandran U, Conti E Structure. 2011 Oct 25. PMID:22032967^[9]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ 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
↑ 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
↑ 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
↑ 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
↑ 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
↑ 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
↑ 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
↑ 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
↑ Jeyaprakash AA, Basquin C, Jayachandran U, Conti E. Structural Basis for the Recognition of Phosphorylated Histone H3 by the Survivin Subunit of the Chromosomal Passenger Complex. Structure. 2011 Oct 25. PMID:22032967 doi:10.1016/j.str.2011.09.002

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4a0j"

@@ Line 1: / Line 1: @@
 ==CRYSTAL STRUCTURE OF SURVIVIN BOUND TO THE PHOSPHORYLATED N-TERMINAL TAIL OF HISTONE H3==
 <StructureSection load='4a0j' size='340' side='right' caption='[[4a0j]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1f3h|1f3h]], [[1e31|1e31]], [[1xox|1xox]], [[4a0i|4a0i]]</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=4a0j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a0j OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4a0j RCSB], [http://www.ebi.ac.uk/pdbsum/4a0j 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=4a0j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a0j OCA], [http://pdbe.org/4a0j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4a0j RCSB], [http://www.ebi.ac.uk/pdbsum/4a0j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4a0j ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4a0j" style="background-color:#fffaf0;"></div>
 ==See Also==

4a0j

From Proteopedia

Revision as of 17:43, 4 August 2016

CRYSTAL STRUCTURE OF SURVIVIN BOUND TO THE PHOSPHORYLATED N-TERMINAL TAIL OF HISTONE H3

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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