Ontology highlight
ABSTRACT:
SUBMITTER: Uysal S
PROVIDER: S-EPMC2672561 | biostudies-literature | 2009 Apr
REPOSITORIES: biostudies-literature
Proceedings of the National Academy of Sciences of the United States of America 20090403 16
KcsA is a proton-activated, voltage-modulated K(+) channel that has served as the archetype pore domain in the Kv channel superfamily. Here, we have used synthetic antigen-binding fragments (Fabs) as crystallographic chaperones to determine the structure of full-length KcsA at 3.8 A, as well as that of its isolated C-terminal domain at 2.6 A. The structure of the full-length KcsA-Fab complex reveals a well-defined, 4-helix bundle that projects approximately 70 A toward the cytoplasm. This bundle ...[more]