The covalent and three-dimensional structure of concanavalin A. II. Amino acid sequence of cyanogen bromide fragment F3.
The covalent and three-dimensional structure of concanavalin A. II. Amino acid sequence of cyanogen bromide fragment F3.
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刀豆球蛋白 A 的共价和三维结构。 II．
DOI：
10.1016/s0021-9258(19)41841-3
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发表时间：
1975
期刊：
影响因子：
--
通讯作者：
G. Edelman
中科院分区：
文献类型：
--
作者：
John L. Wang;B. A. Cunningham;M. Waxdal;G. Edelman
已建立伴刀豆球蛋白A的COOH-末端CNBr片段F3（残基130至237）的氨基酸序列，完成了该凝集素的共价结构的测定。化学序列的分析表明，带电残基的分布一般是更密集的NH 2-末端的一半的多肽链比在COOH-末端部分，在后者的区域有一个线性伸展组成的许多疏水残基。与X-射线晶体学结果的相关性表明，疏水区域位于分子的内部，并且它形成了深腔的一部分，该深腔是抑制剂β-（邻碘苯基）-D-吡喃葡萄糖苷的结合位点。结合三维结构，这里报道的氨基酸序列提供了新的数据分析的变量参与预测的三维折叠的蛋白质的一级结构。伴刀豆球蛋白A的序列是第一个确定的凝集素，它作为一个参考结构与其他凝集素的比较。
The amino acid sequence of the COOH-terminal CNBr fragment, F3 (residues 130 to 237), of concanavalin A has been established, completing the determination of the covalent structure of this lectin. Analysis of the chemical sequence showed that the distribution of charged residues is generally more dense in the NH2-terminal half of the polypeptide chain than in the COOH-terminal portion and that in the latter region there is a linear stretch composed of many hydrophobic residues. Correlation with x-ray crystallographic results indicates that the hydrophobic region is located in the interior of the molecule, and that it forms a part of a deep cavity which is the binding site for the inhibitor, beta-(o-iodophenyl)-D-glucopyranoside. In conjunction with the three-dimensional structure, the amino acid sequence reported here provides new data for analysis of variables involved in predicting the three-dimensional folding of proteins from the primary structure. The sequence of concanavalin A is the first determined for a lectin and it serves as a reference structure for comparisons with other lectins.