2OVC

Crystal structure of a coiled-coil tetramerization domain from Kv7.4 channels

Summary for 2OVC

• Entry DOI: 10.2210/pdb2ovc/pdb
• Descriptor: Potassium voltage-gated channel subfamily KQT member 4 (2 entities in total)
• Functional Keywords: voltage-gated channel, potassium channel, ion channel assembly, coiled-coil, tetramer, transport protein
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 3738.40

Authors

Howard, R.J.,Clark, K.A.,Holton, J.M.,Minor, D.L. (deposition date: 2007-02-13, release date: 2007-03-13, Last modification date: 2024-02-21)

Primary citation

Howard, R.J.,Clark, K.A.,Holton, J.M.,Minor, D.L.
Structural Insight into KCNQ (Kv7) Channel Assembly and Channelopathy.
Neuron, 53:663-675, 2007

PubMed Abstract: Kv7.x (KCNQ) voltage-gated potassium channels form the cardiac and auditory I(Ks) current and the neuronal M-current. The five Kv7 subtypes have distinct assembly preferences encoded by a C-terminal cytoplasmic assembly domain, the A-domain Tail. Here, we present the high-resolution structure of the Kv7.4 A-domain Tail together with biochemical experiments that show that the domain is a self-assembling, parallel, four-stranded coiled coil. Structural analysis and biochemical studies indicate conservation of the coiled coil in all Kv7 subtypes and that a limited set of interactions encode assembly specificity determinants. Kv7 mutations have prominent roles in arrhythmias, deafness, and epilepsy. The structure together with biochemical data indicate that A-domain Tail arrhythmia mutations cluster on the solvent-accessible surface of the subunit interface at a likely site of action for modulatory proteins. Together, the data provide a framework for understanding Kv7 assembly specificity and the molecular basis of a distinct set of Kv7 channelopathies.

PubMed: 17329207
DOI: 10.1016/j.neuron.2007.02.010

Experimental method

X-RAY DIFFRACTION (2.07 Å)