1sqk

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[[Image:1sqk.gif|left|200px]]
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{{Seed}}
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{{STRUCTURE_1sqk| PDB=1sqk | SCENE= }}
{{STRUCTURE_1sqk| PDB=1sqk | SCENE= }}
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'''CRYSTAL STRUCTURE OF CIBOULOT IN COMPLEX WITH SKELETAL ACTIN'''
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===CRYSTAL STRUCTURE OF CIBOULOT IN COMPLEX WITH SKELETAL ACTIN===
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==Overview==
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The widespread beta-thymosin/WH2 actin binding domain has versatile regulatory properties in actin dynamics and motility. beta-thymosins (isolated WH2 domain) maintain monomeric actin in a "sequestered" nonpolymerizable form. In contrast, when repeated in tandem or inserted in modular proteins, the beta-thymosin/WH2 domain promotes actin assembly at filament barbed ends, like profilin. The structural basis for these opposite functions is addressed using ciboulot, a three beta-thymosin repeat protein. Only the first repeat binds actin and possesses the function of ciboulot. The region that shows the strongest interaction with actin is an amphipathic N-terminal alpha helix, present in all beta-thymosin/WH2 domains, which recognizes the ATP bound actin structure and uses the shear motion of actin linked to ATP hydrolysis to control polymerization. Crystallographic ((1)H, (15)N), NMR, and mutagenetic data reveal that the weaker interaction of the C-terminal region of beta-thymosin/WH2 domain with actin accounts for the switch in function from inhibition to promotion of actin assembly.
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(as it appears on PubMed at http://www.pubmed.gov), where 15163409 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15163409}}
==About this Structure==
==About this Structure==
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[[Category: Ciboulot]]
[[Category: Ciboulot]]
[[Category: Wh2 domain]]
[[Category: Wh2 domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:01:25 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 09:57:08 2008''

Revision as of 06:57, 28 July 2008

Image:1sqk.png

Template:STRUCTURE 1sqk

CRYSTAL STRUCTURE OF CIBOULOT IN COMPLEX WITH SKELETAL ACTIN

Template:ABSTRACT PUBMED 15163409

About this Structure

1SQK is a Protein complex structure of sequences from Drosophila melanogaster and Oryctolagus cuniculus. Full crystallographic information is available from OCA.

Reference

The beta-thymosin/WH2 domain; structural basis for the switch from inhibition to promotion of actin assembly., Hertzog M, van Heijenoort C, Didry D, Gaudier M, Coutant J, Gigant B, Didelot G, Preat T, Knossow M, Guittet E, Carlier MF, Cell. 2004 May 28;117(5):611-23. PMID:15163409

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