当前位置: X-MOL 学术Proc. Natl. Acad. Sci. U.S.A. › 论文详情
Supertertiary protein structure affects an allosteric network [Biophysics and Computational Biology]
Proceedings of the National Academy of Sciences of the United States of America ( IF 9.412 ) Pub Date : 2020-09-14 , DOI: 10.1073/pnas.2007201117
Louise Laursen, Johanna Kliche, Stefano Gianni, Per Jemth

The notion that protein function is allosterically regulated by structural or dynamic changes in proteins has been extensively investigated in several protein domains in isolation. In particular, PDZ domains have represented a paradigm for these studies, despite providing conflicting results. Furthermore, it is still unknown how the association between protein domains in supramodules, consitituting so-called supertertiary structures, affects allosteric networks. Here, we experimentally mapped the allosteric network in a PDZ:ligand complex, both in isolation and in the context of a supramodular structure, and show that allosteric networks in a PDZ domain are highly dependent on the supertertiary structure in which they are present. This striking sensitivity of allosteric networks to the presence of adjacent protein domains is likely a common property of supertertiary structures in proteins. Our findings have general implications for prediction of allosteric networks from primary and tertiary structures and for quantitative descriptions of allostery.

更新日期:2020-09-15

 

全部期刊列表>>
物理学研究前沿热点精选期刊推荐
chemistry
《自然》编辑与您分享如何成为优质审稿人-信息流
欢迎报名注册2020量子在线大会
化学领域亟待解决的问题
材料学研究精选新
GIANT
自然职场线上招聘会
ACS ES&T Engineering
科研绘图
ACS ES&T Water
ACS Publications填问卷
屿渡论文,编辑服务
阿拉丁试剂right
张晓晨
田蕾蕾
李闯创
刘天飞
隐藏1h前已浏览文章
课题组网站
新版X-MOL期刊搜索和高级搜索功能介绍
ACS材料视界
天合科研
x-mol收录
X-MOL
苏州大学
廖矿标
深圳湾
试剂库存
down
wechat
bug