Ontology highlight
ABSTRACT:
SUBMITTER: Shah C
PROVIDER: S-EPMC3979964 | biostudies-literature | 2014 Mar
REPOSITORIES: biostudies-literature
Shah Claudio C Hegde Balachandra G BG Morén Björn B Behrmann Elmar E Mielke Thorsten T Moenke Gregor G Spahn Christian M T CMT Lundmark Richard R Daumke Oliver O Langen Ralf R
Structure (London, England : 1993) 20140206 3
The dynamin-related Eps15-homology domain-containing protein 2 (EHD2) is a membrane-remodeling ATPase that regulates the dynamics of caveolae. Here, we established an electron paramagnetic resonance (EPR) approach to characterize structural features of membrane-bound EHD2. We show that residues at the tip of the helical domain can insert into the membrane and may create membrane curvature by a wedging mechanism. Using EPR and X-ray crystallography, we found that the N terminus is folded into a h ...[more]