CRYSTAL-STRUCTURE OF THE 10TH TYPE-III CELL-ADHESION MODULE OF HUMAN FIBRONECTIN
CRYSTAL-STRUCTURE OF THE 10TH TYPE-III CELL-ADHESION MODULE OF HUMAN FIBRONECTIN
复制标题
DOI：
10.1016/0022-2836(94)90013-2
复制
发表时间：
1994-03-04
影响因子：
5.6
通讯作者：
ELY, KR
中科院分区：
文献类型：
--
作者：
DICKINSON, CD;VEERAPANDIAN, B;ELY, KR
纤连蛋白细胞粘附模块 (FNIII 10) 的晶体结构已以 1· 8 Å 分辨率测定。对应于人纤连蛋白第十III型模块的重组片段在空间群P2 1 中结晶，其中a=30·，b=35·1，c=37·7Å，β=107°。通过分子置换确定结构并通过最小二乘法精修。对于 10 至 1·8 Å 数据，91 个氨基酸模块加 56 个溶剂原子的最终模型的晶体学 R-factpr 为 0·18。该模块由两层β-折叠组成，一层具有三个反平行链，另一层具有四个反平行链。 β-折叠包含 24 个氨基酸侧链的疏水核心。该模块在连接两条 β 链的柔性环中包含 RGD 细胞识别序列。 FNIII 10 模块的三级结构已用于开发纤连蛋白中 17 个 III 型模块的基于结构的序列比对，基于同源疏水残基的显着保守性。在与纤连蛋白无关的蛋白质（例如细胞因子受体和肌肉蛋白）中的 III 型模块的比较中，类似的同源交替疏水残基模式也很明显。
The crystal structure of the cell adhesion module of fibronectin (FNIII 10) _has been determined at 1· 8 Å resolution. A recombinant fragment corresponding to the tenth type III module of human fibronectin was crystallized in space group P2 1 with a= 30·, b= 35· 1 and c= 37· 7 A ̊ and β= 107°. The structure was determined by molecular replacement and refined by least squares methods. The crystallographic R-factpr for the final model of the 91 amino acid module plus 56 solvent atoms is 0· 18 for 10 to 1· 8 Å data. The module consists of two layers of β-sheet, one with three antiparallel strands and the other with four antiparallel strands. The β-sheets enclose a hydrophobic core of 24 amino acid side-chains. The module contains the RGD cell recognition sequence in a flexible loop connecting two β-strands. The tertiary structure of the FNIII 10 module has been used to develop a structure-based sequence alignment of 17 type III modules in fibronectin based on the striking conservation of homologous hydrophobic residues. A similar pattern of homologous alternating hydrophobic residues is also evident in a comparison of type III modules in proteins unrelated to fibronectin such as cytokine receptors and muscle proteins.