3u9d: Difference between revisions

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'''Unreleased structure'''
[[Image:3u9d.jpg|left|200px]]


The entry 3u9d is ON HOLD
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{{STRUCTURE_3u9d|  PDB=3u9d |  SCENE=  }}


Authors: Renault, L., Husson, C., Carlier, M.F., Didry, D.
===Crystal Structure of a chimera containing the N-terminal domain (residues 8-24) of drosophila Ciboulot and the C-terminal domain (residues 13-44) of bovine Thymosin-beta4, bound to G-actin-ATP===


Description: Crystal Structure of a chimera containing the N-terminal domain (residues 8-24) of drosophila Ciboulot and the C-terminal domain (residues 13-44) of bovine Thymosin-beta4, bound to G-actin-ATP
 
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{{ABSTRACT_PUBMED_22193718}}
 
==About this Structure==
[[3u9d]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster,bos_taurus Drosophila melanogaster,bos taurus] and [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U9D OCA].
 
==Reference==
<ref group="xtra">PMID:022193718</ref><ref group="xtra">PMID:015163409</ref><references group="xtra"/>
[[Category: Drosophila melanogaster,bos taurus]]
[[Category: Rattus norvegicus]]
[[Category: Carlier, M F.]]
[[Category: Didry, D.]]
[[Category: Husson, C.]]
[[Category: Renault, L.]]
[[Category: Contractile protein]]
[[Category: Protein binding]]

Revision as of 06:32, 25 January 2012

File:3u9d.jpg

Template:STRUCTURE 3u9d

Crystal Structure of a chimera containing the N-terminal domain (residues 8-24) of drosophila Ciboulot and the C-terminal domain (residues 13-44) of bovine Thymosin-beta4, bound to G-actin-ATP

Template:ABSTRACT PUBMED 22193718

About this Structure

3u9d is a 4 chain structure with sequence from Drosophila melanogaster,bos taurus and Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

  1. Didry D, Cantrelle FX, Husson C, Roblin P, Moorthy AM, Perez J, Le Clainche C, Hertzog M, Guittet E, Carlier MF, van Heijenoort C, Renault L. How a single residue in individual beta-thymosin/WH2 domains controls their functions in actin assembly. EMBO J. 2011 Dec 23. doi: 10.1038/emboj.2011.461. PMID:22193718 doi:10.1038/emboj.2011.461
  2. Hertzog M, van Heijenoort C, Didry D, Gaudier M, Coutant J, Gigant B, Didelot G, Preat T, Knossow M, Guittet E, Carlier MF. The beta-thymosin/WH2 domain; structural basis for the switch from inhibition to promotion of actin assembly. Cell. 2004 May 28;117(5):611-23. PMID:15163409

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