Construction of a model for the aggregation and cross‐linking region (7S domain) of type IV collagen based upon an evaluation of the primary structure of the α1 and α2 chains in this region
Construction of a model for the aggregation and cross‐linking region (7S domain) of type IV collagen based upon an evaluation of the primary structure of the α1 and α2 chains in this region
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基于对 IV 型胶原蛋白聚集和交联区域（7S 结构域）的 α1 和 α2 链一级结构的评估，构建该区域的模型
DOI：
10.1111/j.1432-1033.1987.tb13455.x
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发表时间：
1987
期刊：
影响因子：
5.4
通讯作者：
K. Kaehn
中科院分区：
文献类型：
--
作者：
B. Siebold;R. Qian;R. Glanville;H. Hofmann;R. Deutzmann;K. Kaehn
给出了人基底膜胶原α2(IV)链N端聚集和交联区212个残基的氨基酸序列。将其与α1(IV)7S的一级结构进行比较[Glanville等人。(1985)欧元。J.生物化学。152,213-219]显示了三个功能区高度相似的亚区。这些是21个残基长的N末端非三螺旋区域(NH1)，含有半胱氨酸和赖氨酸残基，这些残基是假定的交联点，117个残基长的三螺旋区域(TH1)负责四个分子聚集形成7S结构域并且也具有交联点，最后是10个残基长的非三螺旋区域(NH2)，它将许多柔性区域中的第一个引入到分子的三螺旋体内[Hofmann等人]。(1984)J.Mol.比奥尔。172、325-343]。通过计算机计算7S结构域平行和反平行排列的三螺旋区域(TH1)之间的相互作用分数，可以预测7S复合体的详细结构模型，该模型与主要基于旋转阴影IV型胶原四聚体电子显微镜的模型吻合良好。结果表明，7S结构域的组装是由疏水相互作用引导的，并自我限制为四聚体。最有利的链型是α2-α1-α1。
The amino acid sequence of the 212-residues-long N-terminal aggregation and cross-linking region of the alpha 2(IV) chain of human basement membrane collagen is presented. Comparing this with the primary structure of alpha 1(IV)7S [Glanville et al. (1985) Eur. J. Biochem. 152, 213-219] revealed a high degree of similar subdivisions in three functional regions. These are the 21-residue-long N-terminal non-triple-helical regions (NH1) containing cysteine and lysine residues which are putative cross-linking sites, a 117-residue-long triple-helical region (TH1) responsible for the aggregation of four molecules to form the 7S domain and which also possess cross-linking sites, and finally a 10-residue-long non-triple-helical region (NH2) which introduces the first of many flexible areas into the triple helical body of the molecule [Hofmann et al. (1984) J. Mol. Biol. 172, 325-343]. Computer calculations of interaction scores between parallel and antiparallelly aligned triple-helical regions (TH1) of the 7S domain allowed the prediction of a detailed model for the structure of the 7S complex which agreed well with models based primarily on electron micrographs of rotary shadowed type IV collagen tetramers. The results indicated that the assembly of the 7S domain is directed by hydrophobic interactions and is self-limiting to a tetramer. The most favourable chain configuration is alpha 2-alpha 1-alpha 1.
来自牛晶状体囊和小鼠肿瘤的基底膜胶原蛋白 α 1 (IV) 链的胃蛋白酶抗性片段的序列比较。
DOI：
10.1042/bj2200227
发表时间：
1984
期刊：
The Biochemical journal
影响因子：
--
作者：
Schuppan,D;Glanville,RW;Timpl,R;Dixit,SN;Kang,AH
通讯作者：
Kang,AH
DOI：
--
发表时间：
1983
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Duncan,KG;Fessler,LI;Bächinger,HP;Fessler,JH
通讯作者：
Fessler,JH
DOI：
--
发表时间：
1982
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Bächinger,HP;Fessler,LI;Fessler,JH
通讯作者：
Fessler,JH