CRYSTAL-STRUCTURE OF TANDEM TYPE-III FIBRONECTIN DOMAINS FROM DROSOPHILA NEUROGLIAN AT 2.0 ANGSTROM
CRYSTAL-STRUCTURE OF TANDEM TYPE-III FIBRONECTIN DOMAINS FROM DROSOPHILA NEUROGLIAN AT 2.0 ANGSTROM
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DOI：
10.1016/0896-6273(94)90326-3
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发表时间：
1994-04-01
期刊：
影响因子：
16.2
通讯作者：
BJORKMAN, PJ
中科院分区：
文献类型：
--
作者：
HUBER, AH;WANG, YME;BJORKMAN, PJ
我们报道了果蝇神经细胞黏附分子神经胶质中两个相邻的纤维连接蛋白III型重复序列的晶体结构。每个结构域由两个反平行的β片断组成，与细胞外基质蛋白Tenascin和FN的单个III型纤维连接蛋白结构域在拓扑上相同地折叠。β凸起和左手多聚脯氨酸II螺旋破坏了这两个神经胶质结构域的规则的β折叠结构。疏水的结构域间界面包括一个金属结合部位，可能参与稳定结构域之间的相对取向，通过序列比较预测存在于脊椎动物同源分子L1中。神经胶质结构域由一个近乎完美的2重螺旋轴沿着最长的分子维度连接起来。利用这种关系，提出了一个在神经胶质和其他分子中串联的纤维连接蛋白III型重复序列的模型。
We report the crystal structure of two adjacent fibronectin type III repeats from the Drosophila neural cell adhesion molecule neuroglian. Each domain consists of two antiparallel beta sheets and is folded topologically identically to single fibronectin type III domains from the extracellular matrix proteins tenascin and fibronectin. beta bulges and left-handed polyproline II helices disrupt the regular beta sheet structure of both neuroglian domains. The hydrophobic interdomain interface includes a metal-binding site, presumably involved in stabilizing the relative orientation between domains and predicted by sequence comparision to be present in the vertebrate homolog molecule L1. The neuroglian domains are related by a near perfect 2-fold screw axis along the longest molecular dimension. Using this relationship, a model for arrays of tandem fibronectin type III repeats in neuroglian and other molecules is proposed.