4D1E

THE CRYSTAL STRUCTURE OF HUMAN MUSCLE ALPHA-ACTININ-2

Summary for 4D1E

• Entry DOI: 10.2210/pdb4d1e/pdb
• Descriptor: ALPHA-ACTININ-2 (1 entity in total)
• Functional Keywords: contractile protein, z-disc, calmodulin-like domain, spectrin domain, actin binding domain, abd
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Cytoplasm, myofibril, sarcomere, Z line : P35609
• Total number of polymer chains: 1
• Total formula weight: 101854.59

Authors

Pinotsis, N.,Salmazo, A.,Sjoeblom, B.,Gkougkoulia, E.,Djinovic-Carugo, K. (deposition date: 2014-05-01, release date: 2014-12-10, Last modification date: 2023-12-20)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (3.5 Å)