3UGU
Crystal Structure of p44 (Splice Variant of Visual Arrestin)
Summary for 3UGU
| Entry DOI | 10.2210/pdb3ugu/pdb |
| Related | 3UGX |
| Descriptor | S-arrestin (2 entities in total) |
| Functional Keywords | arrestin fold, signal termination, gpcr, outer segment, signaling protein |
| Biological source | Bos taurus (bovine) |
| Total number of polymer chains | 1 |
| Total formula weight | 42417.76 |
| Authors | Batra-Safferling, R.,Granzin, J. (deposition date: 2011-11-03, release date: 2012-02-08, Last modification date: 2024-02-28) |
| Primary citation | Granzin, J.,Cousin, A.,Weirauch, M.,Schlesinger, R.,Buldt, G.,Batra-Safferling, R. Crystal Structure of p44, a Constitutively Active Splice Variant of Visual Arrestin. J.Mol.Biol., 416:611-618, 2012 Cited by PubMed Abstract: Visual arrestin specifically binds to photoactivated and phosphorylated rhodopsin and inactivates phototransduction. In contrast, the p44 splice variant can terminate phototransduction by binding to nonphosphorylated light-activated rhodopsin. Here we report the crystal structure of bovine p44 at a resolution of 1.85 Å. Compared to native arrestin, the p44 structure reveals significant differences in regions crucial for receptor binding, namely flexible loop V-VI and polar core regions. Additionally, electrostatic potential is remarkably positive on the N-domain and the C-domain. The p44 structure represents an active conformation that serves as a model to explain the 'constitutive activity' found in arrestin variants. PubMed: 22306737DOI: 10.1016/j.jmb.2012.01.028 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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