3jve

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{{STRUCTURE_3jve| PDB=3jve | SCENE= }}
{{STRUCTURE_3jve| PDB=3jve | SCENE= }}
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===Crystal Structure of the Sixth BRCT Domain of TopBP1===
===Crystal Structure of the Sixth BRCT Domain of TopBP1===
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{{ABSTRACT_PUBMED_19937654}}
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==Function==
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[[http://www.uniprot.org/uniprot/TOPB1_HUMAN TOPB1_HUMAN]] Required for DNA replication. Plays a role in the rescue of stalled replication forks and checkpoint control. Binds double-stranded DNA breaks and nicks as well as single-stranded DNA. Recruits the SWI/SNF chromatin remodeling complex to E2F1-responsive promoters. Down-regulates E2F1 activity and inhibits E2F1-dependent apoptosis during G1/S transition and after DNA damage. Induces a large increase in the kinase activity of ATR.<ref>PMID:10498869</ref><ref>PMID:11395493</ref><ref>PMID:11714696</ref><ref>PMID:12697828</ref><ref>PMID:15075294</ref><ref>PMID:16530042</ref>
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{{ABSTRACT_PUBMED_19937654}}
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==About this Structure==
==About this Structure==
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3JVE is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JVE OCA].
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[[3jve]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JVE OCA].
==Reference==
==Reference==
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<ref group="xtra">PMID:19937654</ref><references group="xtra"/>
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<ref group="xtra">PMID:019937654</ref><references group="xtra"/><references/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Baker, D.]]
[[Category: Baker, D.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 10 14:12:14 2010''
 

Revision as of 09:17, 27 March 2013

Template:STRUCTURE 3jve

Contents

Crystal Structure of the Sixth BRCT Domain of TopBP1

Template:ABSTRACT PUBMED 19937654

Function

[TOPB1_HUMAN] Required for DNA replication. Plays a role in the rescue of stalled replication forks and checkpoint control. Binds double-stranded DNA breaks and nicks as well as single-stranded DNA. Recruits the SWI/SNF chromatin remodeling complex to E2F1-responsive promoters. Down-regulates E2F1 activity and inhibits E2F1-dependent apoptosis during G1/S transition and after DNA damage. Induces a large increase in the kinase activity of ATR.[1][2][3][4][5][6]

About this Structure

3jve is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

  • Leung CC, Kellogg E, Kuhnert A, Hanel F, Baker D, Glover JN. Insights from the crystal structure of the sixth BRCT domain of topoisomerase IIbeta binding protein 1. Protein Sci. 2010 Jan;19(1):162-7. PMID:19937654 doi:10.1002/pro.290
  1. ↑ Yamane K, Tsuruo T. Conserved BRCT regions of TopBP1 and of the tumor suppressor BRCA1 bind strand breaks and termini of DNA. Oncogene. 1999 Sep 16;18(37):5194-203. PMID:10498869 doi:10.1038/sj.onc.1202922
  2. ↑ Makiniemi M, Hillukkala T, Tuusa J, Reini K, Vaara M, Huang D, Pospiech H, Majuri I, Westerling T, Makela TP, Syvaoja JE. BRCT domain-containing protein TopBP1 functions in DNA replication and damage response. J Biol Chem. 2001 Aug 10;276(32):30399-406. Epub 2001 Jun 6. PMID:11395493 doi:10.1074/jbc.M102245200
  3. ↑ Honda Y, Tojo M, Matsuzaki K, Anan T, Matsumoto M, Ando M, Saya H, Nakao M. Cooperation of HECT-domain ubiquitin ligase hHYD and DNA topoisomerase II-binding protein for DNA damage response. J Biol Chem. 2002 Feb 1;277(5):3599-605. Epub 2001 Nov 19. PMID:11714696 doi:10.1074/jbc.M104347200
  4. ↑ Liu K, Lin FT, Ruppert JM, Lin WC. Regulation of E2F1 by BRCT domain-containing protein TopBP1. Mol Cell Biol. 2003 May;23(9):3287-304. PMID:12697828
  5. ↑ Liu K, Luo Y, Lin FT, Lin WC. TopBP1 recruits Brg1/Brm to repress E2F1-induced apoptosis, a novel pRb-independent and E2F1-specific control for cell survival. Genes Dev. 2004 Mar 15;18(6):673-86. PMID:15075294 doi:10.1101/gad.1180204
  6. ↑ Kumagai A, Lee J, Yoo HY, Dunphy WG. TopBP1 activates the ATR-ATRIP complex. Cell. 2006 Mar 10;124(5):943-55. PMID:16530042 doi:10.1016/j.cell.2005.12.041

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