1PRW
Crystal structure of bovine brain Ca++ calmodulin in a compact form
Summary for 1PRW
Entry DOI | 10.2210/pdb1prw/pdb |
Related | 1CDL 1CDM 1CLN |
Descriptor | Calmodulin, CALCIUM ION (3 entities in total) |
Functional Keywords | ef hand, calcium-binding protein, kinase activator, metal binding protein |
Biological source | Bos taurus (cattle) |
Cellular location | Cytoplasm: P62157 |
Total number of polymer chains | 1 |
Total formula weight | 16949.78 |
Authors | Fallon, J.L.,Quiocho, F.A. (deposition date: 2003-06-20, release date: 2003-10-10, Last modification date: 2011-07-13) |
Primary citation | Fallon, J.L.,Quiocho, F.A. A closed compact structure of native ca(2+)-calmodulin. Structure, 11:1303-1307, 2003 Cited by PubMed Abstract: Calmodulin has been a subject of intense scrutiny since its discovery because of its unusual properties in regulating the functions of about 100 diverse target enzymes and structural proteins. The original and to date only crystal conformation of native eukaryotic Ca(2+)-calmodulin (Ca(2+)-CaM) is a very extended molecule with two widely separated globular domains linked by an exposed long helix. Here we report the 1.7 A X-ray structure of a new native Ca(2+)-CaM that is in a compact ellipsoidal conformation and shows a sharp bend in the linker helix and a more contracted N-terminal domain. This conformation may offer advantages for recognition of kinase-type calmodulin targets or small organic molecule drugs. PubMed: 14527397DOI: 10.1016/j.str.2003.09.004 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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