2ff3: Difference between revisions

Revision as of 07:18, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2ff3.png

Template:STRUCTURE 2ff3

Crystal structure of Gelsolin domain 1:N-wasp V2 motif hybrid in complex with actinCrystal structure of Gelsolin domain 1:N-wasp V2 motif hybrid in complex with actin

Template:ABSTRACT PUBMED 16531231

About this StructureAbout this Structure

2FF3 is a Protein complex structure of sequences from 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 Mon Jul 28 07:18:15 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:2ff3.gif|left|200px]]
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-'''Crystal structure of Gelsolin domain 1:N-wasp V2 motif hybrid in complex with actin'''
+===Crystal structure of Gelsolin domain 1:N-wasp V2 motif hybrid in complex with actin===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_16531231}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16531231 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_16531231}}
 ==About this Structure==
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 [[Category: Xue, B.]]
 [[Category: Protein-protein complex]]
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