Ontology highlight
ABSTRACT:
SUBMITTER: Vamvouka M
PROVIDER: S-EPMC2248300 | biostudies-literature | 2008 Mar
REPOSITORIES: biostudies-literature
Vamvouka Magdalini M Cieslak John J Van Eps Ned N Hubbell Wayne W Gross Adrian A
Protein science : a publication of the Protein Society 20080301 3
A four-pulse electron paramagnetic resonance experiment was used to measure long-range inter-subunit distances in reconstituted KvAP, a voltage-dependent potassium (Kv) channel. The measurements have allowed us to reach the following five conclusions about the native structure of the voltage sensor of KvAP. First, the S1 helix of the voltage sensor engages in a helix packing interaction with the pore domain. Second, the crystallographically observed antiparallel helix-turn-helix motif of the vol ...[more]