1QUU
CRYSTAL STRUCTURE OF TWO CENTRAL SPECTRIN-LIKE REPEATS FROM ALPHA-ACTININ
Summary for 1QUU
| Entry DOI | 10.2210/pdb1quu/pdb |
| Descriptor | HUMAN SKELETAL MUSCLE ALPHA-ACTININ 2 (2 entities in total) |
| Functional Keywords | triple-helix coiled coil, contractile protein |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm, myofibril, sarcomere, Z line : P35609 |
| Total number of polymer chains | 1 |
| Total formula weight | 29283.83 |
| Authors | Djinovic-Carugo, K.,Young, P.,Gautel, M.,Saraste, M. (deposition date: 1999-07-03, release date: 1999-08-20, Last modification date: 2024-02-14) |
| Primary citation | Djinovic-Carugo, K.,Young, P.,Gautel, M.,Saraste, M. Structure of the alpha-actinin rod: molecular basis for cross-linking of actin filaments. Cell(Cambridge,Mass.), 98:537-546, 1999 Cited by PubMed Abstract: We have determined the crystal structure of the two central repeats in the alpha-actinin rod at 2.5 A resolution. The repeats are connected by a helical linker and form a symmetric, antiparallel dimer in which the repeats are aligned rather than staggered. Using this structure, which reveals the structural principle that governs the architecture of alpha-actinin, we have devised a plausible model of the entire alpha-actinin rod. The electrostatic properties explain how the two alpha-actinin subunits assemble in an antiparallel fashion, placing the actin-binding sites at both ends of the rod. This molecular architecture results in a protein that is able to form cross-links between actin filaments. PubMed: 10481917DOI: 10.1016/S0092-8674(00)81981-9 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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