The two polypeptide chains in fibronectin are joined in antiparallel fashion: NMR structural characterization.
The two polypeptide chains in fibronectin are joined in antiparallel fashion: NMR structural characterization.
复制标题
纤连蛋白中的两条多肽链以反平行方式连接：NMR 结构表征。
DOI：
10.1021/bi00156a010
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发表时间：
1992
期刊：
影响因子：
2.9
通讯作者：
Llinás,M
中科院分区：
文献类型：
--
作者：
An,SS;Jiménez-Barbero,J;Petersen,TE;Llinás,M
1992年7月23日收到的修订版Mandarin pt摘要：通过1H NMR光谱法在水和二甲基亚砜（DMSO）溶液中研究了纤连蛋白C-末端链间二硫键连接的七肽二聚体（Val-Asn-Cys-Pro-Ile-Glu-Cys）2。在DMSO中的质子Overhauser实验明确地表明，两条纤连蛋白多肽链以反平行的方式首尾相连（N-末端到C-末端）。发现肽的结构被延伸。从~ 1H NMR的质子间距离和角度的限制，优选的平均（时间平均）的构象在H_2O和DMSO推导出使用距离几何和分子力学算法。这两种构象虽然明显不同，但都表现出结构平行的共同特征。纤连蛋白是一种分子量约为440 000 M的双链糖蛋白，存在于血浆、细胞表面、组织内结缔组织基质、血管和基底膜中。（McDonagh，1985; Vartio & Vahari，1983; Mosher，1989; Ruoslahti，1988）。两条链α和β是高度同源的，并且各自由重复的球状模块的串联阵列组成，一般称为I型、II型和III型结构域（Skorstengaard等人，1986年）。纤连蛋白是一种粘附性多功能蛋白质，其识别广泛的底物，包括纤维蛋白、肝素、明胶、胶原和细胞表面。因此，它参与了多种细胞
Revised Manuscript Received July 23, 1992 abstract: The fibronectin C-terminal interchain disulfide-linked heptapeptide dimer (Val-Asn-Cys-Pro-Ile-Glu-Cys) 2 has been investigated via'H NMR spectroscopy in both water and dimethyl sulfoxide (DMSO) solutions. Proton Overhauser experiments in DMSO indicateunambiguously that thetwo fibronectin polypeptide chains are linked head-to-tail (N-terminus to C-terminus), in an antiparallel fashion. It is found that the structure of the peptide is extended. From the ‘H NMR interproton distanceand angle constraints, the preferred mean (time-averaged) conformations in both H2O and DMSO were derived using distance geometry and molecular mechanics algorithms. The two conformations, althoughsignificantly dissimilar, exhibit the common feature of a structurally parallel (as opposed to chemically antiparallel) fibronectin a/0 chain array.Fibronectin is a two-chain glycoprotein of~ 440 000 M, found in blood plasma, cell surfaces, intratissue connective matrix, blood vessels, andbasement membranes (McDonagh, 1985; Vartio & Vahari, 1983; Mosher, 1989; Ruoslahti, 1988). The two chains, a and 0, are highly homologousand are each composed of a tandem array of repeated globular modules, generically known as type I, type II, and type III domains (Skorstengaard et al., 1986). Fibronectin is an adhesive multifunctional protein, which recognizes a wide spectrum of substrates, including fibrin, heparin, gelatin, collagen, and cell surfaces. As such, it is involved in a variety of cellular