引用本文:
You Qi TANG, Gen Pei LI, Zhong Guo CHEN, Jie ZENG, Tien Chin TSAO, Guang Da LIN, Rong Guang ZHANG, Zheng Wu CHI. CRYSTAL STRUCTURE OF THE COMPLEX OF MUNG BEAN TRYPSIN INHIBITOR LYSINE ACTIVE FRAGMENT WITH BOVINE TRYPSIN AT 1.8 ÅRESOLUTION[J]. Chinese Chemical Letters,
1990, 1(1): 61-64.
Citation: You Qi TANG, Gen Pei LI, Zhong Guo CHEN, Jie ZENG, Tien Chin TSAO, Guang Da LIN, Rong Guang ZHANG, Zheng Wu CHI. CRYSTAL STRUCTURE OF THE COMPLEX OF MUNG BEAN TRYPSIN INHIBITOR LYSINE ACTIVE FRAGMENT WITH BOVINE TRYPSIN AT 1.8 ÅRESOLUTION[J]. Chinese Chemical Letters, 1990, 1(1): 61-64.
Citation: You Qi TANG, Gen Pei LI, Zhong Guo CHEN, Jie ZENG, Tien Chin TSAO, Guang Da LIN, Rong Guang ZHANG, Zheng Wu CHI. CRYSTAL STRUCTURE OF THE COMPLEX OF MUNG BEAN TRYPSIN INHIBITOR LYSINE ACTIVE FRAGMENT WITH BOVINE TRYPSIN AT 1.8 ÅRESOLUTION[J]. Chinese Chemical Letters, 1990, 1(1): 61-64.
CRYSTAL STRUCTURE OF THE COMPLEX OF MUNG BEAN TRYPSIN INHIBITOR LYSINE ACTIVE FRAGMENT WITH BOVINE TRYPSIN AT 1.8 ÅRESOLUTION
摘要:
The structure of the complex of mung bean trypsin inhibitor lysine active fragment with bovine trypsin has been determined at a resolution of 1.8 Å by A-ray crystallographic analysis and the complex model refined by restrained least-squares minimization with the data between 10 Å and 1.8 Å resolution.The current conventional R factor is 17.3%, and the model con-tains 1648 protein atoms, 219 inhibitor atoms and 126 water molecules.Themost prominent feature of the inhibitor fragment is that it does not containany alpha-helices.Most of the chain fold in an irregular fashion.The seven residues of the binding segment of the inhibitor lysine active frag-ment are in specific contact with bovine trypsin.The binding interactionand geometry around the reactive site are similar to that observed in otherstudies of trypsin-inhibitor complexes.
English
CRYSTAL STRUCTURE OF THE COMPLEX OF MUNG BEAN TRYPSIN INHIBITOR LYSINE ACTIVE FRAGMENT WITH BOVINE TRYPSIN AT 1.8 ÅRESOLUTION
Abstract:
The structure of the complex of mung bean trypsin inhibitor lysine active fragment with bovine trypsin has been determined at a resolution of 1.8 Å by A-ray crystallographic analysis and the complex model refined by restrained least-squares minimization with the data between 10 Å and 1.8 Å resolution.The current conventional R factor is 17.3%, and the model con-tains 1648 protein atoms, 219 inhibitor atoms and 126 water molecules.Themost prominent feature of the inhibitor fragment is that it does not containany alpha-helices.Most of the chain fold in an irregular fashion.The seven residues of the binding segment of the inhibitor lysine active frag-ment are in specific contact with bovine trypsin.The binding interactionand geometry around the reactive site are similar to that observed in otherstudies of trypsin-inhibitor complexes.
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