2ff6: Difference between revisions

Revision as of 03:49, 4 May 2008

Crystal structure of Gelsolin domain 1:ciboulot domain 2 hybrid in complex with actin

OverviewOverview

Participation of actin in cellular processes relies on the dynamics of filament assembly. Filament elongation is fed by monomeric actin in complex with either profilin or a Wiscott-Aldrich syndrome protein (WASP) homology domain 2 (WH2)/beta-thymosin (betaT) domain. WH2/betaT motif repetition (typified by ciboulot) or combination with nonrelated domains (as found in N-WASP) results in proteins that yield their actin to filament elongation. Here, we report the crystal structures of actin bound hybrid proteins, constructed between gelsolin and WH2/betaT domains from ciboulot or N-WASP. We observe the C-terminal half of ciboulot domain 2 bound to actin. In solution, we show that cibolout domains 2 and 3 bind to both G- and F-actin, and that whole ciboulot forms a complex with two actin monomers. In contrast, the analogous portion of N-WASP WH2 domain 2 is detached from actin, indicating that the C-terminal halves of the betaT and WH2 motifs are not functionally analogous.

About this StructureAbout this Structure

2FF6 is a Protein complex structure of sequences from Drosophila melanogaster, Homo sapiens and Oryctolagus cuniculus. Full crystallographic information is available from OCA.

ReferenceReference

The structural basis of actin interaction with multiple WH2/beta-thymosin motif-containing proteins., Aguda AH, Xue B, Irobi E, Preat T, Robinson RC, Structure. 2006 Mar;14(3):469-76. PMID:16531231 Page seeded by OCA on Sun May 4 03:49:32 2008

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OCA

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 '''Crystal structure of Gelsolin domain 1:ciboulot domain 2 hybrid in complex with actin'''
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-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:01:59 2008''