Ontology highlight
ABSTRACT:
SUBMITTER: Zhou Q
PROVIDER: S-EPMC3974213 | biostudies-literature | 2014 Mar
REPOSITORIES: biostudies-literature
Zhou Qiangjun Q Li Jiangmei J Yu Hang H Zhai Yujia Y Gao Zhen Z Liu Yanxin Y Pang Xiaoyun X Zhang Lunfeng L Schulten Klaus K Sun Fei F Chen Chang C
Nature communications 20140328
Phosphatidylinositol 4-kinase IIα (PI4KIIα), a membrane-associated PI kinase, plays a central role in cell signalling and trafficking. Its kinase activity critically depends on palmitoylation of its cysteine-rich motif (-CCPCC-) and is modulated by the membrane environment. Lack of atomic structure impairs our understanding of the mechanism regulating kinase activity. Here we present the crystal structure of human PI4KIIα in ADP-bound form. The structure identifies the nucleotide-binding pocket ...[more]