与抑制蛋白与磷酸化、光解视紫红质的功能性结合相关的抑制蛋白残基。
Arrestin residues involved in the functional binding of arrestin to phosphorylated, photolyzed rhodopsin.
作者信息
Ascano Maria T, Smith W Clay, Gregurick Susan K, Robinson Phyllis R
机构信息
Department of Biological Sciences, University of Maryland, Baltimore County, Baltimore, MD 21250, USA.
出版信息
Mol Vis. 2006 Dec 5;12:1516-25.
PURPOSE
The purpose of our study was to determine whether arrestin residues previously predicted by computational modeling to interact with an aspartic acid substituted rhodopsin tail are actually involved in interactions with phospho-residues on the rhodopsin cytoplasmic tail.
METHODS
We generated arrestin mutants with altered charges at predicted positions. These mutants were then tested for the ability to inhibit rhodopsin using both direct binding assays, as well as functional assays involving transducin inhibition assays.
RESULTS
Our results demonstrate that the computer-predicted residues are indeed involved in both the ability of the low-affinity state of arrestin to bind to rhodopsin as well as the ability of arrestin to be induced into a higher-affinity state in a phospho-residue-dependent manner.
CONCLUSIONS
Our results also suggest that positions K14, K15, R29, H301, and K300 on arrestin interact with the phosphorylated carboxyl tail of rhodopsin and that this translates to the efficient activation of arrestin.
目的
我们研究的目的是确定先前通过计算模型预测与天冬氨酸取代的视紫红质尾巴相互作用的抑制蛋白残基是否实际上参与了与视紫红质细胞质尾巴上磷酸化残基的相互作用。
方法
我们在预测位置产生了电荷改变的抑制蛋白突变体。然后使用直接结合测定以及涉及转导素抑制测定的功能测定来测试这些突变体抑制视紫红质的能力。
结果
我们的结果表明，计算机预测的残基确实参与了抑制蛋白低亲和力状态与视紫红质结合的能力，以及抑制蛋白以磷酸化残基依赖性方式被诱导为高亲和力状态的能力。
结论
我们的结果还表明，抑制蛋白上的K14、K15、R29、H301和K300位置与视紫红质的磷酸化羧基尾巴相互作用，并且这转化为抑制蛋白的有效激活。
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