Unknown

Dataset Information

0

Structure of the KvAP voltage-dependent K+ channel and its dependence on the lipid membrane.


ABSTRACT: Voltage-dependent ion channels gate open in response to changes in cell membrane voltage. This form of gating permits the propagation of action potentials. We present two structures of the voltage-dependent K(+) channel KvAP, in complex with monoclonal Fv fragments (3.9 A) and without antibody fragments (8 A). We also studied KvAP with disulfide cross-bridges in lipid membranes. Analyzing these data in the context of the crystal structure of Kv1.2 and EPR data on KvAP we reach the following conclusions: (i) KvAP is similar in structure to Kv1.2 with a very modest difference in the orientation of its voltage sensor; (ii) mAb fragments are not the source of non-native conformations of KvAP in crystal structures; (iii) because KvAP contains separate loosely adherent domains, a lipid membrane is required to maintain their correct relative orientations, and (iv) the model of KvAP is consistent with the proposal of voltage sensing through the movement of an arginine-containing helix-turn-helix element at the protein-lipid interface.

SUBMITTER: Lee SY 

PROVIDER: S-EPMC1253646 | biostudies-literature |

REPOSITORIES: biostudies-literature

Similar Datasets

| S-EPMC1304651 | biostudies-literature
| S-EPMC2847477 | biostudies-literature
| S-EPMC4047412 | biostudies-literature
| S-EPMC7768720 | biostudies-literature
| S-EPMC7403406 | biostudies-literature
| S-EPMC6882556 | biostudies-literature
| S-EPMC3827124 | biostudies-literature
| S-EPMC3137058 | biostudies-literature
| S-EPMC2614752 | biostudies-literature
| S-EPMC6317592 | biostudies-literature