1HCI

CRYSTAL STRUCTURE OF THE ROD DOMAIN OF ALPHA-ACTININ

Summary for 1HCI

Entry DOI	10.2210/pdb1hci/pdb
Related	1H8B 1QUU
Descriptor	ALPHA-ACTININ 2 (2 entities in total)
Functional Keywords	triple-helix coiled coil, contractile protein, muscle, z-line, actin-binding protein
Biological source	HOMO SAPIENS (HUMAN)
Cellular location	Cytoplasm, myofibril, sarcomere, Z line: P35609
Total number of polymer chains	2
Total formula weight	112422.65
Authors	Ylanne, J.,Scheffzek, K.,Young, P.,Saraste, M. (deposition date: 2001-05-04, release date: 2001-06-27, Last modification date: 2023-12-13)
Primary citation	Ylanne, J.,Scheffzek, K.,Young, P.,Saraste, M. Crystal Structure of the Alpha-Actinin Rod Reveals an Extensive Torsional Twist Structure, 9:597-, 2001 Cited by PubMed Abstract: Alpha-actinin is a ubiquitously expressed protein found in numerous actin structures. It consists of an N-terminal actin binding domain, a central rod domain, and a C-terminal domain and functions as a homodimer to cross-link actin filaments. The rod domain determines the distance between cross-linked actin filaments and also serves as an interaction site for several cytoskeletal and signaling proteins. PubMed: 11470434 DOI: 10.1016/S0969-2126(01)00619-0 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.8 Å)

Structure validation