Ontology highlight
ABSTRACT:
SUBMITTER: Xiong JP
PROVIDER: S-EPMC2733745 | biostudies-literature | 2009 Aug
REPOSITORIES: biostudies-literature
Xiong Jian-Ping JP Mahalingham Bhuvaneshwari B Alonso Jose Luis JL Borrelli Laura Ann LA Rui Xianliang X Anand Saurabh S Hyman Bradley T BT Rysiok Thomas T Müller-Pompalla Dirk D Goodman Simon L SL Arnaout M Amin MA
The Journal of cell biology 20090801 4
We determined the crystal structure of 1TM-alphaVbeta3, which represents the complete unconstrained ectodomain plus short C-terminal transmembrane stretches of the alphaV and beta3 subunits. 1TM-alphaVbeta3 is more compact and less active in solution when compared with DeltaTM-alphaVbeta3, which lacks the short C-terminal stretches. The structure reveals a bent conformation and defines the alpha-beta interface between IE2 (EGF-like 2) and the thigh domains. Modifying this interface by site-direc ...[more]