4bry

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==About this Structure==
==About this Structure==
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[[4bry]] is a 2 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=4BRY OCA].
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[[4bry]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BRY OCA].
==Reference==
==Reference==
<ref group="xtra">PMID:024064211</ref><references group="xtra"/><references/>
<ref group="xtra">PMID:024064211</ref><references group="xtra"/><references/>
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[[Category: Homo sapiens]]
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[[Category: Human]]
[[Category: Caillat, C.]]
[[Category: Caillat, C.]]
[[Category: Perrakis, A.]]
[[Category: Perrakis, A.]]
[[Category: Cell cycle]]
[[Category: Cell cycle]]
[[Category: Dna replication licensing]]
[[Category: Dna replication licensing]]

Revision as of 11:44, 20 November 2013

Template:STRUCTURE 4bry

Contents

The Idas:Geminin heterodimeric parallel coiled-coil

Template:ABSTRACT PUBMED 24064211

Function

[GEMI_HUMAN] Inhibits DNA replication by preventing the incorporation of MCM complex into pre-replication complex (pre-RC). It is degraded during the mitotic phase of the cell cycle. Its destruction at the metaphase-anaphase transition permits replication in the succeeding cell cycle.[1] [2] [3] Inhibits the transcriptional activity of a subset of Hox proteins, enrolling them in cell proliferative control.[4] [5] [6] [MCIN_HUMAN] Transcription regulator required for multiciliate cell differentiation. Acts by promoting transcription of genes required for multiciliate cell formation. Probably acts in a multiprotein complex (By similarity). Plays a role in mitotic cell cycle progression by promoting cell cycle exit.

About this Structure

4bry is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA.

Reference

  • Caillat C, Pefani ED, Gillespie PJ, Taraviras S, Blow JJ, Lygerou Z, Perrakis A. The Geminin and Idas coiled coils preferentially form a heterodimer that inhibits Geminin function in DNA replication licensing. J Biol Chem. 2013 Oct 2. PMID:24064211 doi:http://dx.doi.org/10.1074/jbc.M113.491928
  1. ↑ McGarry TJ, Kirschner MW. Geminin, an inhibitor of DNA replication, is degraded during mitosis. Cell. 1998 Jun 12;93(6):1043-53. PMID:9635433
  2. ↑ Sugimoto N, Tatsumi Y, Tsurumi T, Matsukage A, Kiyono T, Nishitani H, Fujita M. Cdt1 phosphorylation by cyclin A-dependent kinases negatively regulates its function without affecting geminin binding. J Biol Chem. 2004 May 7;279(19):19691-7. Epub 2004 Mar 1. PMID:14993212 doi:10.1074/jbc.M313175200
  3. ↑ Zhou B, Liu C, Xu Z, Zhu G. Structural basis for homeodomain recognition by the cell-cycle regulator Geminin. Proc Natl Acad Sci U S A. 2012 May 21. PMID:22615398 doi:10.1073/pnas.1200874109
  4. ↑ McGarry TJ, Kirschner MW. Geminin, an inhibitor of DNA replication, is degraded during mitosis. Cell. 1998 Jun 12;93(6):1043-53. PMID:9635433
  5. ↑ Sugimoto N, Tatsumi Y, Tsurumi T, Matsukage A, Kiyono T, Nishitani H, Fujita M. Cdt1 phosphorylation by cyclin A-dependent kinases negatively regulates its function without affecting geminin binding. J Biol Chem. 2004 May 7;279(19):19691-7. Epub 2004 Mar 1. PMID:14993212 doi:10.1074/jbc.M313175200
  6. ↑ Zhou B, Liu C, Xu Z, Zhu G. Structural basis for homeodomain recognition by the cell-cycle regulator Geminin. Proc Natl Acad Sci U S A. 2012 May 21. PMID:22615398 doi:10.1073/pnas.1200874109

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