Crystal structure of the functional unit of interphotoreceptor retinoid binding protein
Crystal structure of the functional unit of interphotoreceptor retinoid binding protein
复制标题
DOI：
10.1016/s0969-2126(01)00698-0
复制
发表时间：
2002-01-01
期刊：
影响因子：
5.7
通讯作者：
Loew, A
中科院分区：
文献类型：
--
作者：
Loew, A
光感受器间维甲酸结合蛋白（IRBP）是光感受器间基质的主要可溶性成分，对脊椎动物视网膜的功能、完整性和发育至关重要。虽然其作用知之甚少，IRBP已被认为保护11-顺式视黄醇和全反式视黄醇，同时促进它们在光感受器和视网膜色素上皮之间的交换。我们确定的X射线结构的一个功能单元，或模块，非洲爪蟾IRBP到1.8埃分辨率的多波长异常色散。单体蛋白质由两个结构域组成，由疏水配体结合位点分开。最近解决的光系统II D1 C-末端加工蛋白酶和烯酰辅酶A异构酶/水合酶家族的结构同源性表明，在不同的设置中使用的一个共同的倍的效用，从蛋白质水解脂肪酸异构化类维生素A运输。
Interphotoreceptor retinoid binding protein (IRBP), the major soluble component of the interphotoreceptor matrix, is critical to the function, integrity, and development of the vertebrate retina. Although its role is poorly understood, IRBP has been thought to protect 11-cis retinal and all-trans retinol while facilitating their exchange between the photoreceptors and retinal-pigmented epithelium. We determined the X-ray structure of one of the functional units, or modules, of Xenopus laevis IRBP to 1.8 Angstrom resolution by multi-wavelength anomalous dispersion. The monomeric protein consists of two domains separated by a hydrophobic ligand binding site. A structural homology to the recently solved photosystem II D1 C-terminal-processing protease and the enoyl-CoA isomerase/hydratase family suggests the utility of a common fold used in diverse settings, ranging from proteolysis to fatty acid isomerization to retinoid transport.