Crystal structure of a complex formed between organic solvent treated bovine alpha-chymotrypsin and its autocatalytically produced highly potent 14-residue peptide at 2.2 resolution

Crystal structure of a complex formed between organic solvent treated bovine alpha-chymotrypsin and its autocatalytically produced highly potent 14-residue peptide at 2.2 resolution Descriptor: Chymotrypsinogen A, SULFATE ION Authors: Singh, N, Jabeen, T, Sharma, S, Roy, I, Gupta, M.N, Bilgrami, S, Singh, T.P. Deposit date: 2003-04-02 Release date: 2004-05-18 Last modified: 2024-10-30 Method: X-RAY DIFFRACTION (2.2 Å) Cite: Detection of native peptides as potent inhibitors of enzymes. Crystal structure of the complex formed between treated bovine alpha-chymotrypsin and an autocatalytically produced fragment, IIe-Val-Asn-Gly-Glu-Glu-Ala-Val-Pro-Gly-Ser-Trp-Pro-Trp, at 2.2 angstroms resolution. Febs J., 272, 2005

经有机溶剂处理的牛源α-胰凝乳蛋白酶（alpha-chymotrypsin）与其自催化产生的强效14残基肽形成的复合物的晶体结构，分辨率为2.2埃
描述物：胰凝乳蛋白酶原A（Chymotrypsinogen A）、硫酸根离子
作者：Singh, N、Jabeen, T、Sharma, S、Roy, I、Gupta, M.N、Bilgrami, S、Singh, T.P.
提交日期：2003年4月2日
发布日期：2004年5月18日
最后修改日期：2024年10月30日
实验方法：X射线衍射（2.2 Å）
引用文献：检测天然肽作为强效酶抑制剂。经处理的牛源α-胰凝乳蛋白酶与自催化产生的片段IIe-Val-Asn-Gly-Glu-Glu-Ala-Val-Pro-Gly-Ser-Trp-Pro-Trp形成的复合物的晶体结构，分辨率为2.2埃。《FEBS期刊》（Febs J.），第272卷，2005年