Ontology highlight
ABSTRACT:
SUBMITTER: Jao CC
PROVIDER: S-EPMC2888429 | biostudies-literature | 2010 Jun
REPOSITORIES: biostudies-literature
Jao Christine C CC Hegde Balachandra G BG Gallop Jennifer L JL Hegde Prabhavati B PB McMahon Harvey T HT Haworth Ian S IS Langen Ralf R
The Journal of biological chemistry 20100423 26
Control of membrane curvature is required in many important cellular processes, including endocytosis and vesicular trafficking. Endophilin is a bin/amphiphysin/rvs (BAR) domain protein that induces vesicle formation by promotion of membrane curvature through membrane binding as a dimer. Using site-directed spin labeling and EPR spectroscopy, we show that the overall BAR domain structure of the rat endophilin A1 dimer determined crystallographically is maintained under predominantly vesiculating ...[more]