1T44

Structural basis of actin sequestration by thymosin-B4: Implications for arp2/3 activation

1T44 の概要

• エントリーDOI: 10.2210/pdb1t44/pdb
• 関連するPDBエントリー: 1P8Z
• 分子名称: Chimera of Gelsolin domain 1 and C-Terminal domain of thymosin Beta-4, Actin, alpha, CALCIUM ION, ... (5 entities in total)
• 機能のキーワード: structural protein
• 由来する生物種: Homo sapiens (human, house mouse); 詳細
• 細胞内の位置: Cytoplasm, cytoskeleton: P20065
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 58533.06

構造登録者

Irobi, E.,Aguda, A.H.,Larsson, M.,Burtnick, L.D.,Robinson, R.C. (登録日: 2004-04-28, 公開日: 2004-09-07, 最終更新日: 2023-08-23)

主引用文献

Irobi, E.,Aguda, A.H.,Larsson, M.,Guerin, C.,Yin, H.L.,Burtnick, L.D.,Blanchoin, L.,Robinson, R.C.
Structural basis of actin sequestration by thymosin-beta4: implications for WH2 proteins.
Embo J., 23:3599-3608, 2004

PubMed 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.

PubMed: 15329672
DOI: 10.1038/sj.emboj.7600372

実験手法

X-RAY DIFFRACTION (2 Å)