1AYR
ARRESTIN FROM BOVINE ROD OUTER SEGMENTS
Summary for 1AYR
| Entry DOI | 10.2210/pdb1ayr/pdb |
| Descriptor | ARRESTIN (2 entities in total) |
| Functional Keywords | sensory transduction, arrestin, rhodopsin |
| Biological source | Bos taurus (cattle) |
| Total number of polymer chains | 4 |
| Total formula weight | 164005.09 |
| Authors | Granzin, J.,Wilden, U.,Choe, H.-W.,Labahn, J.,Krafft, B.,Bueldt, G. (deposition date: 1997-11-10, release date: 1998-11-25, Last modification date: 2024-02-07) |
| Primary citation | Granzin, J.,Wilden, U.,Choe, H.W.,Labahn, J.,Krafft, B.,Buldt, G. X-ray crystal structure of arrestin from bovine rod outer segments. Nature, 391:918-921, 1998 Cited by PubMed Abstract: Retinal arrestin is the essential protein for the termination of the light response in vertebrate rod outer segments. It plays an important role in quenching the light-induced enzyme cascade by its ability to bind to phosphorylated light-activated rhodopsin (P-Rh*). Arrestins are found in various G-protein-coupled amplification cascades. Here we report on the three-dimensional structure of bovine arrestin (relative molecular mass, 45,300) at 3.3 A resolution. The crystal structure comprises two domains of antiparallel beta-sheets connected through a hinge region and one short alpha-helix on the back of the amino-terminal fold. The binding region for phosphorylated light-activated rhodopsin is located at the N-terminal domain, as indicated by the docking of the photoreceptor to the three-dimensional structure of arrestin. This agrees with the interpretation of binding studies on partially digested and mutated arrestin. PubMed: 9495348DOI: 10.1038/36147 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.3 Å) |
Structure validation
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