1. |
|
|
2. |
- Irobi, Edward, et al.
(författare)
-
Structural basis of actin sequestration by thymosin β4 : implications for WH2 proteins
- 2004
-
Ingår i: EMBO Journal. - : Wiley. - 0261-4189 .- 1460-2075. ; 23:18, s. 3599-608
-
Tidskriftsartikel (refereegranskat)abstract
- The WH2 (Wiscott-Aldridge syndrome protein homology domain 2) repeat is an actin interacting motif found in monomer sequestering and filament assembly proteins. We have stabilized the prototypical WH2 family member, thymosin-beta4 (Tbeta4), with respect to actin, by creating a hybrid between gelsolin domain 1 and the C-terminal half of Tbeta4 (G1-Tbeta4). This hybrid protein sequesters actin monomers, severs actin filaments and acts as a leaky barbed end cap. Here, we present the structure of the G1-Tbeta4:actin complex at 2 A resolution. The structure reveals that Tbeta4 sequesters by capping both ends of the actin monomer, and that exchange of actin between Tbeta4 and profilin is mediated by a minor overlap in binding sites. The structure implies that multiple WH2 motif-containing proteins will associate longitudinally with actin filaments. Finally, we discuss the role of the WH2 motif in arp2/3 activation.
|
|
3. |
|
|