4D1E

THE CRYSTAL STRUCTURE OF HUMAN MUSCLE ALPHA-ACTININ-2

4D1E の概要

• エントリーDOI: 10.2210/pdb4d1e/pdb
• 分子名称: ALPHA-ACTININ-2 (1 entity in total)
• 機能のキーワード: contractile protein, z-disc, calmodulin-like domain, spectrin domain, actin binding domain, abd
• 由来する生物種: HOMO SAPIENS (HUMAN)
• 細胞内の位置: Cytoplasm, myofibril, sarcomere, Z line : P35609
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 101854.59

構造登録者

Pinotsis, N.,Salmazo, A.,Sjoeblom, B.,Gkougkoulia, E.,Djinovic-Carugo, K. (登録日: 2014-05-01, 公開日: 2014-12-10, 最終更新日: 2023-12-20)

主引用文献

Ribeiro Jr, E.A.,Pinotsis, N.,Ghisleni, A.,Salmazo, A.,Konarev, P.V.,Kostan, J.,Sjoeblom, B.,Schreiner, C.,Polyansky, A.A.,Gkougkoulia, E.,Holt, M.R.,Aachmann, F.L.,Zagrovic, B.,Bordignon, E.,Pirker, K.F.,Svergun, D.I.,Gautel, M.,Djinovic-Carugo, K.
The Structure and Regulation of Human Muscle Alpha-Actinin
Cell(Cambridge,Mass.), 159:1447-, 2014

PubMed Abstract: The spectrin superfamily of proteins plays key roles in assembling the actin cytoskeleton in various cell types, crosslinks actin filaments, and acts as scaffolds for the assembly of large protein complexes involved in structural integrity and mechanosensation, as well as cell signaling. α-actinins in particular are the major actin crosslinkers in muscle Z-disks, focal adhesions, and actin stress fibers. We report a complete high-resolution structure of the 200 kDa α-actinin-2 dimer from striated muscle and explore its functional implications on the biochemical and cellular level. The structure provides insight into the phosphoinositide-based mechanism controlling its interaction with sarcomeric proteins such as titin, lays a foundation for studying the impact of pathogenic mutations at molecular resolution, and is likely to be broadly relevant for the regulation of spectrin-like proteins.

PubMed: 25433700
DOI: 10.1016/J.CELL.2014.10.056

実験手法

X-RAY DIFFRACTION (3.5 Å)