4D1E: The Crystal Structure Of Human Muscle Alpha-actinin-2

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. alpha-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 alpha-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.
PDB ID: 4D1EDownload
MMDB ID: 125370
PDB Deposition Date: 2014/5/1
Updated in MMDB: 2014/12
Experimental Method:
x-ray diffraction
Resolution: 3.5  Å
Source Organism:
Similar Structures:
Biological Unit for 4D1E: dimeric; determined by author and by software (PISA)
Molecular Components in 4D1E
Label Count Molecule
Proteins (2 molecules)
Alpha-actinin-2(Gene symbol: ACTN2)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB