|本期目录/Table of Contents|

[1]岳耀敬,刘建斌,郭婷婷,等.抑制素α亚基三级结构与其他TGF-β配体的比较[J].江苏农业科学,2014,42(10):32-36.
 Yue Yaojing,et al.Comparison of tertiary structure of inhibin αsubunit and other TGF-β ligands[J].Jiangsu Agricultural Sciences,2014,42(10):32-36.
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抑制素α亚基三级结构与其他TGF-β配体的比较(PDF)
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《江苏农业科学》[ISSN:1002-1302/CN:32-1214/S]

卷:
第42卷
期数:
2014年10期
页码:
32-36
栏目:
生物技术
出版日期:
2014-10-25

文章信息/Info

Title:
Comparison of tertiary structure of inhibin αsubunit and other TGF-β ligands
作者:
岳耀敬 刘建斌 郭婷婷 郭宪 郭健 孙晓萍 杨博辉
中国农业科学院兰州畜牧与兽药研究所,甘肃兰州 730050
Author(s):
Yue Yaojinget al
关键词:
抑制素α亚基3D结构模拟TGF-β结构特征
Keywords:
-
分类号:
Q75
DOI:
-
文献标志码:
A
摘要:
抑制素A和抑制素B是由不同抑制素/激活素β亚基(βA、βB)和结构相似的α亚基组成的同源二聚体,即抑制素A (αβA)、抑制素B(αβB)。利用生物信息学技术对抑制素α亚基(INHα)进行三级结构建模,并利用ClustalW和SPDV软件比较INHα与其他转化生长因子β(TGF-β)超结构家族成员在结构和序列方面的异同。结果表明,激活素(ACT)、骨形成蛋白7(BMP7)、BMP9与type Ⅱ受体结合面的核心氨基酸在INH α 中不仅在多处发生了突变,而且在空间上也发生了很大位移,因此如果INH α同时与type Ⅱ受体在与激活素、BMP7、BMP9的相同位置结合,那么INH α会比激活素与激活素受体ActRⅡ、ActRⅡB的亲和力低。ACT A中几个参与活化素受体样激酶4(ALK4)相互作用的氨基酸在INH α中发生了突变,ACT A α螺旋中极性氨基酸在INH α 中被非极性氨基酸所替代,且α 螺旋在空间上发生了很大位移,INH α 不与ALK4结合。可见,抑制素信号传导机制为:抑制素与Betaglycan高亲和力结合并与ActR Ⅱ、ActR ⅡB、BMPR Ⅱ形成复合物,但不与ALK4结合,因此将它们与激活素和BMP隔离。
Abstract:
-

参考文献/References:

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备注/Memo

备注/Memo:
收稿日期:2013-12-11
基金项目:甘肃省青年自然科学基金(编号:1308RJYA037)。
作者简介:岳耀敬(1980—),男,山东聊城人,博士研究生,助理研究员,研究方向为动物遗传育种与繁殖。Tel:(0931)2115173;E-mail:yueyaojing@caas.cn。
更新日期/Last Update: 2014-10-25