3u9z: Difference between revisions

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'''Unreleased structure'''
[[Image:3u9z.jpg|left|200px]]


The entry 3u9z is ON HOLD until Paper Publication
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{{STRUCTURE_3u9z|  PDB=3u9z  |  SCENE=  }}


Authors: Renault, L., Husson, C., Carlier, M.F., Didry, D.
===Crystal structure between actin and a protein construct containing the first beta-thymosin domain of drosophila ciboulot (residues 2-58) with the three mutations N26D/Q27K/D28S===


Description: Crystal structure between actin and a protein construct containing the first beta-thymosin domain of drosophila ciboulot (residues 2-58) with the three mutations N26D/Q27K/D28S
 
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{{ABSTRACT_PUBMED_22193718}}
 
==About this Structure==
[[3u9z]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] and [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U9Z OCA].
 
==Reference==
<ref group="xtra">PMID:022193718</ref><ref group="xtra">PMID:015163409</ref><references group="xtra"/>
[[Category: Drosophila melanogaster]]
[[Category: Oryctolagus cuniculus]]
[[Category: Carlier, M F.]]
[[Category: Didry, D.]]
[[Category: Husson, C.]]
[[Category: Renault, L.]]
[[Category: Contractile protein]]
[[Category: Protein binding]]

Revision as of 06:35, 25 January 2012

File:3u9z.jpg

Template:STRUCTURE 3u9z

Crystal structure between actin and a protein construct containing the first beta-thymosin domain of drosophila ciboulot (residues 2-58) with the three mutations N26D/Q27K/D28S

Template:ABSTRACT PUBMED 22193718

About this Structure

3u9z is a 2 chain structure with sequence from Drosophila melanogaster and Oryctolagus cuniculus. 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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