当前位置: X-MOL 学术ACS Pharmacol. Transl. Sci. › 论文详情
Identification of Key Structural Motifs Involved in 7 Transmembrane Signaling of Adhesion GPCRs
ACS Pharmacology & Translational Science Pub Date : 2019-02-15 , DOI: 10.1021/acsptsci.8b00051
Marta Arimont, Melanie van der Woude, Rob Leurs, Henry F. Vischer, Chris de Graaf, Saskia Nijmeijer

The adhesion class B2 family of G protein-coupled receptors (GPCRs) plays a key role in important physiological processes and their dysfunction is linked to brain malformations and tumorigenesis. Although information regarding their signaling properties is starting to emerge, the structural motifs and interaction networks that determine 7 transmembrane (TM) signaling of class B2 GPCRs remain to be elucidated. Comparative sequence–structure analyses of class B2 GPCRs and the recently solved active class B1 structures show that class B2 GPCRs include different elements of the conserved residue motifs that determine class B1 activation. Combined site-directed mutagenesis and molecular dynamics studies were performed to give detailed insights into the role of 7TM interaction networks in signaling of two representative class B2 receptors, ADGRG1 (GPR56) and ADGRL4 (ELTD1). The systematic investigation of class B1/B2 sequence motifs provides consistent structure–function relationships that can be translated to the whole class B2 GPCR family and suggests that class B1 and B2 GPCRs share conserved intramolecular 7TM interactions. This improved understanding in adhesion GPCR structure and constitutive signaling can accelerate drug design campaigns for this chemically unexplored receptor class.
更新日期:2019-04-01

 

全部期刊列表>>
chemistry
物理学研究前沿热点精选期刊推荐
自然职位线上招聘会
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
ACS ES&T Engineering
ACS ES&T Water
ACS Publications填问卷
屿渡论文,编辑服务
阿拉丁试剂right
南昌大学
王辉
南方科技大学
彭小水
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
赵延川
李霄羽
廖矿标
朱守非
试剂库存
down
wechat
bug