Ontology highlight
ABSTRACT:
SUBMITTER: Luca VC
PROVIDER: S-EPMC5459593 | biostudies-literature | 2017 Mar
REPOSITORIES: biostudies-literature
Luca Vincent C VC Kim Byoung Choul BC Ge Chenghao C Kakuda Shinako S Wu Di D Roein-Peikar Mehdi M Haltiwanger Robert S RS Zhu Cheng C Ha Taekjip T Garcia K Christopher KC
Science (New York, N.Y.) 20170302 6331
Notch receptor activation initiates cell fate decisions and is distinctive in its reliance on mechanical force and protein glycosylation. The 2.5-angstrom-resolution crystal structure of the extracellular interacting region of Notch1 complexed with an engineered, high-affinity variant of Jagged1 (Jag1) reveals a binding interface that extends ~120 angstroms along five consecutive domains of each protein. <i>O</i>-Linked fucose modifications on Notch1 epidermal growth factor-like (EGF) domains 8 ...[more]