1TJT

X-ray structure of the human alpha-actinin isoform 3 at 2.2A resolution

1TJT の概要

• エントリーDOI: 10.2210/pdb1tjt/pdb
• 関連するPDBエントリー: 1AOA 1DXX 1MB8 1QAG 1WKU
• 分子名称: Alpha-actinin 3 (2 entities in total)
• 機能のキーワード: calponin homology domain, actin binding domain, contractile protein
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 28620.84

構造登録者

Franzot, G.,Sjoblom, B.,Gautel, M.,Djinovic Carugo, K. (登録日: 2004-06-07, 公開日: 2005-05-17, 最終更新日: 2023-10-25)

主引用文献

Franzot, G.,Sjoblom, B.,Gautel, M.,Djinovic Carugo, K.
The crystal structure of the actin binding domain from alpha-actinin in its closed conformation: structural insight into phospholipid regulation of alpha-actinin
J.Mol.Biol., 348:151-165, 2005

PubMed Abstract: Alpha-actinin is the major F-actin crosslinking protein in both muscle and non-muscle cells. We report the crystal structure of the actin binding domain of human muscle alpha-actinin-3, which is formed by two consecutive calponin homology domains arranged in a "closed" conformation. Structural studies and available biochemical data on actin binding domains suggest that two calponin homology domains come in a closed conformation in the native apo-form, and that conformational changes involving the relative orientation of the two calponin homology domains are required for efficient binding to actin filaments. The actin binding activity of muscle isoforms is supposed to be regulated by phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), which binds to the second calponin homology domain. On the basis of structural analysis we propose a distinct binding site for PtdIns(4,5)P2, where the fatty acid moiety would be oriented in a direction that allows it to interact with the linker sequence between the actin binding domain and the first spectrin-like repeat, regulating thereby the binding of the C-terminal calmodulin-like domain to this linker.

PubMed: 15808860
DOI: 10.1016/j.jmb.2005.01.002

実験手法

X-RAY DIFFRACTION (2.19 Å)