Stability and specificity of protein-protein interactions: the case of the trypsin-trypsin inhibitor complexes.

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作者信息

Janin J, Chothia C

出版信息

J Mol Biol. 1976 Jan 15;100(2):197-211. doi: 10.1016/s0022-2836(76)80148-9.

DOI:10.1016/s0022-2836(76)80148-9

PMID:943547

Abstract

摘要

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Stability and specificity of protein-protein interactions: the case of the trypsin-trypsin inhibitor complexes.

J Mol Biol. 1976 Jan 15;100(2):197-211. doi: 10.1016/s0022-2836(76)80148-9.

Crystal structure of the complex of porcine trypsin with soybean trypsin inhibitor (Kunitz) at 2.6-A resolution.猪胰蛋白酶与大豆胰蛋白酶抑制剂（库尼兹）复合物在2.6埃分辨率下的晶体结构。

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Pre-existence of the active site in zymogens, the interaction of trypsinogen with the basic pancreatic trypsin inhibitor (Kunitz).酶原中活性位点的预先存在，胰蛋白酶原与碱性胰腺胰蛋白酶抑制剂（库尼茨）的相互作用。

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The involvement of an arginine residue of trypsin in its interaction with the Kunitz soybean trypsin inhibitor.胰蛋白酶的一个精氨酸残基在其与库尼茨大豆胰蛋白酶抑制剂相互作用中的参与情况。

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[X-ray structure analyses of proteinase inhibitors].

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Replacement of lysine by arginine, phenylalanine and tryptophan in the reactive site of the bovine trypsin-kallikrein inhibitor (Kunitz) and change of the inhibitory properties.牛胰蛋白酶-激肽释放酶抑制剂（Kunitz）活性位点中赖氨酸被精氨酸、苯丙氨酸和色氨酸取代及其抑制特性的改变。

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Kinetics of binding of bovine trypsin-killikrein inhibitor (K unitz) in which the reactive-site peptide bond Lys-15--Ala-16 is cleaved, to alpha-chymotrypsin and beta-trypsin.牛胰蛋白酶-激肽释放酶抑制剂（K单位）（其中活性位点肽键Lys-15--Ala-16被裂解）与α-胰凝乳蛋白酶和β-胰蛋白酶结合的动力学。

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