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The transition of bovine trypsinogen to a trypsin-like state upon strong ligand binding. The refined crystal structures of the bovine trypsinogen-pancreatic trypsin inhibitor complex and of its ternary complex with Ile-Val at 1.9 A resolution.

作者信息

Bode W, Schwager P, Huber R

出版信息

J Mol Biol. 1978 Jan 5;118(1):99-112. doi: 10.1016/0022-2836(78)90246-2.

DOI:10.1016/0022-2836(78)90246-2
PMID:625059
Abstract
摘要

相似文献

1
The transition of bovine trypsinogen to a trypsin-like state upon strong ligand binding. The refined crystal structures of the bovine trypsinogen-pancreatic trypsin inhibitor complex and of its ternary complex with Ile-Val at 1.9 A resolution.强配体结合时牛胰蛋白酶原向类胰蛋白酶状态的转变。牛胰蛋白酶原 - 胰蛋白酶抑制剂复合物及其与异亮氨酸 - 缬氨酸的三元复合物在1.9埃分辨率下的精细晶体结构。
J Mol Biol. 1978 Jan 5;118(1):99-112. doi: 10.1016/0022-2836(78)90246-2.
2
Zymogen activation: effect of peptides sequentially related to the bovine beta-trypsin N-terminus on Kazal inhibitor and benzamidine binding to bovine trypsinogen.酶原激活：与牛β-胰蛋白酶N端序列相关的肽对卡扎尔抑制剂和苯甲脒与牛胰蛋白酶原结合的影响
J Mol Recognit. 1988 Jun;1(3):130-7. doi: 10.1002/jmr.300010306.
3
The refined 2.2-A (0.22-nm) X-ray crystal structure of the ternary complex formed by bovine trypsinogen, valine-valine and the Arg15 analogue of bovine pancreatic trypsin inhibitor.
Eur J Biochem. 1984 Oct 1;144(1):185-90. doi: 10.1111/j.1432-1033.1984.tb08447.x.
4
Hydrogen exchange kinetics of bovine pancreatic trypsin inhibitor beta-sheet protons in trypsin-bovine pancreatic trypsin inhibitor, trypsinogen-bovine pancreatic trypsin inhibitor, and trypsinogen-isoleucylvaline-bovine pancreatic trypsin inhibitor.胰蛋白酶-牛胰蛋白酶抑制剂、胰蛋白酶原-牛胰蛋白酶抑制剂以及胰蛋白酶原-异亮氨酰缬氨酸-牛胰蛋白酶抑制剂中牛胰蛋白酶抑制剂β-折叠质子的氢交换动力学
Biochemistry. 1987 Jun 2;26(11):3156-67. doi: 10.1021/bi00385a032.
5
Binding of the Ile-Val and Val-Val effector dipeptides to the binary adducts of bovine trypsinogen with Kunitz and Kazal inhibitors as well as the acylating agent p-nitrophenyl p-guanidinobenzoate. A thermodynamic and kinetic study.异亮氨酸-缬氨酸和缬氨酸-缬氨酸效应二肽与牛胰蛋白酶原与库尼兹和卡扎尔抑制剂以及酰化剂对硝基苯基对胍基苯甲酸酯的二元加合物的结合。一项热力学和动力学研究。
J Mol Biol. 1987 Apr 20;194(4):751-4. doi: 10.1016/0022-2836(87)90253-1.
6
Bovine trypsinogen activation. A thermodynamic study.
Biophys Chem. 1990 Aug 31;37(1-3):355-62. doi: 10.1016/0301-4622(90)88034-p.
7
Trypsin activation. Effect of the Ile-Val dipeptide concentration on Kazal inhibitor binding to bovine trypsinogen.胰蛋白酶激活。异亮氨酸-缬氨酸二肽浓度对卡扎尔抑制剂与牛胰蛋白酶原结合的影响。
Biochim Biophys Acta. 1985 Dec 20;832(3):378-82. doi: 10.1016/0167-4838(85)90274-2.
8
Interaction between squash inhibitors and bovine trypsinogen.南瓜抑制剂与牛胰蛋白酶原之间的相互作用。
Biol Chem Hoppe Seyler. 1991 Apr;372(4):255-62. doi: 10.1515/bchm3.1991.372.1.255.
9
Three-dimensional structure of the complex between pancreatic secretory trypsin inhibitor (Kazal type) and trypsinogen at 1.8 A resolution. Structure solution, crystallographic refinement and preliminary structural interpretation.分辨率为1.8埃时，胰腺分泌型胰蛋白酶抑制剂（卡扎尔型）与胰蛋白酶原复合物的三维结构。结构解析、晶体学精修及初步结构阐释。
J Mol Biol. 1982 Dec 25;162(4):839-68. doi: 10.1016/0022-2836(82)90550-2.
10
Structure of bovine trypsinogen at 1.9 A resolution.分辨率为1.9埃的牛胰蛋白酶原结构。
Biochemistry. 1977 Feb 22;16(4):654-64. doi: 10.1021/bi00623a016.

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