کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2030405 | 1071101 | 2006 | 8 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: The Structural Basis of Actin Interaction with Multiple WH2/β-Thymosin Motif-Containing Proteins The Structural Basis of Actin Interaction with Multiple WH2/β-Thymosin Motif-Containing Proteins](/preview/png/2030405.png)
SummaryParticipation 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)/β-thymosin (βT) domain. WH2/βT 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/βT 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 βT and WH2 motifs are not functionally analogous.
Journal: - Volume 14, Issue 3, March 2006, Pages 469–476