Crystal Structure of p44, a Constitutively Active Splice Variant of Visual Arrestin

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• 作者：Joachim Granzin¹ ; Anneliese Cousin² ; Moritz Weirauch² ; Ramona Schlesinger² ; ³ ; Georg Bü ; ldt² ; ⁴ ; Renu Batra-Safferling¹ ; ^{r.batra-safferling@fz-juelich.de}
• 关键词：Rh?/sup> ; light-activated rhodopsin ; P-Rh?/sup> ; light-activated phosphorylated rhodopsin ; P-Rh ; phosphorylated rhodopsin ; ROS ; rod outer segment ; PDB ; Protein Data Bank
• 刊名：Journal of Molecular Biology
• 出版年：2012
• 出版时间：9 March, 2012
• 年：2012
• 卷：416
• 期：5
• 页码：611-618
• 全文大小：1072 K

文摘

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??. 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.