Silk gland-specific proteinase inhibitor serpin16 from the Bombyx mori shows cysteine proteinase inhibitory activity

被引:19
作者
Guo, Peng-Chao [1 ]
Dong, Zhaoming [1 ]
Xiao, Li [1 ]
Li, Tao [1 ]
Zhang, Yan [1 ]
He, Huawei [1 ]
Xia, Qingyou [1 ]
Zhao, Ping [1 ]
机构
[1] Southwest Univ, State Key Lab Silkworm Genome Biol, Chongqing 400716, Peoples R China
基金
中国博士后科学基金; 中国国家自然科学基金;
关键词
Serpin (serine proteinase inhibitor); Bombyx mori; Silk gland-specific; Inhibitory activity; Structure; AMINO-ACID-SEQUENCE; SWISS-MODEL; HEMOLYMPH ANTITRYPSIN; PROTEASE COMPLEX; REACTIVE CENTER; ANTI-THROMBIN; MANDUCA-SEXTA; HOMOLOGY; OVALBUMIN; SUPERFAMILY;
D O I
10.1016/j.bbrc.2014.12.056
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Serpins (serine proteinase inhibitors) are widely distributed in different species and are well known for their inhibitory activities towards serine proteinases. Here, we report the functional characterization of Bombyx mori serpin16. Expression analysis showed that serpin16 was specifically expressed at high levels in the silk gland at both the transcriptional and translational levels. Moreover, homology modeling and multi-sequence alignment suggested that serpin16 had a canonical serpin fold, but it contained a unique reactive center loop, which was obviously shorter than that of typical serpins. Inhibitory activity analyses revealed that the target proteinase of serpinl 8 is a cysteine proteinase, rather than a serine proteinase. Furthermore, a Michaelis complex model of serpin16 with its target proteinase was constructed to explain the structural basis of how serpin16 recognizes the cysteine proteinase and its target specificity. (C) 2014 Elsevier Inc. All rights reserved.
引用
收藏
页码:31 / 36
页数:6
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