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Citation: Tang Youqi, Zeng Jie, Chen Zhongguo, Li Genpei, Lu Guangying, Wei Xincheng, Cao Tienchin, Lin Guangda, Zhang Rongguang, Xuan Jiancheng, Chi Zhengwu. CRYSTAL STRUCTURE ANALYSIS AND MOLECULAR MODEL OF MUNG BEAN TRYPSIN INHIBITOR LYS ACTIVE FRAGMANT—BOVINE TRYPSIN (MBILFBTRY) COMPLEX AT 0.3 nm RESOLUTION[J]. Acta Physico-Chimica Sinica, ;1986, 2(03): 195-198. doi: 10.3866/PKU.WHXB19860302 shu

CRYSTAL STRUCTURE ANALYSIS AND MOLECULAR MODEL OF MUNG BEAN TRYPSIN INHIBITOR LYS ACTIVE FRAGMANT—BOVINE TRYPSIN (MBILFBTRY) COMPLEX AT 0.3 nm RESOLUTION

1.
Institute of Physical Chemistry and Department of Biology, Peking University; Institute of Biochemistry, Academic Sinica, Shanghai

Received Date: 20 March 1986
Available Online: 15 June 1986

Crystal structure of MBILF-BTRY complex was successfully solved by molecular replacement method and its 3-dimensional molecular model was thereby derived.
Mung bean trypsin inhibitor belongs to Bowman-Birk inhibitor group, which is by far the most complicated among the ten fundamental groups of serine protease inhibitor. Neither the 3-dimensional structure of Bowman-Birk inhibitor group nor the stereoscopic conformation of its complex with protease has ever been reported. The crystallographic data of MBILF-BTRY complex are found to be a=....
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