2ff3
From Proteopedia
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Crystal structure of Gelsolin domain 1:N-wasp V2 motif hybrid in complex with actin
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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.
Disease
Known disease associated with this structure: Amyloidosis, Finnish type OMIM:[137350]
About this Structure
2FF3 is a Protein complex structure of sequences from Homo sapiens and Oryctolagus cuniculus with CA and ATP as ligands. Full crystallographic information is available from OCA.
Reference
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 Nov 12 22:04:22 2007
