1ZTO

INACTIVATION GATE OF POTASSIUM CHANNEL RCK4, NMR, 8 STRUCTURES

Summary for 1ZTO

• Entry DOI: 10.2210/pdb1zto/pdb
• Descriptor: POTASSIUM CHANNEL PROTEIN RCK4 (1 entity in total)
• Functional Keywords: potassium channel, inactivation gate
• Biological source: Homo sapiens (human)
• Cellular location: Membrane; Multi-pass membrane protein: P15385
• Total number of polymer chains: 1
• Total formula weight: 4116.63

Authors

Antz, C.,Geyer, M.,Fakler, B.,Schott, M.,Frank, R.,Guy, H.R.,Ruppersberg, J.P.,Kalbitzer, H.R. (deposition date: 1996-11-15, release date: 1997-06-05, Last modification date: 2022-03-02)

Primary citation

Antz, C.,Geyer, M.,Fakler, B.,Schott, M.K.,Guy, H.R.,Frank, R.,Ruppersberg, J.P.,Kalbitzer, H.R.
NMR structure of inactivation gates from mammalian voltage-dependent potassium channels.
Nature, 385:272-275, 1997

PubMed Abstract: The electrical signalling properties of neurons originate largely from the gating properties of their ion channels. N-type inactivation of voltage-gated potassium (Kv) channels is the best-understood gating transition in ion channels, and occurs by a 'ball-and-chain' type mechanism. In this mechanism an N-terminal domain (inactivation gate), which is tethered to the cytoplasmic side of the channel protein by a protease-cleavable chain, binds to its receptor at the inner vestibule of the channel, thereby physically blocking the pore. Even when synthesized as a peptide, ball domains restore inactivation in Kv channels whose inactivation domains have been deleted. Using high-resolution nuclear magnetic resonance (NMR) spectroscopy, we analysed the three-dimensional structure of the ball peptides from two rapidly inactivating mammalian K. channels (Raw3 (Kv3.4) and RCK4 (Kv1.4)). The inactivation peptide of Raw3 (Raw3-IP) has a compact structure that exposes two phosphorylation sites and allows the formation of an intramolecular disulphide bridge between two spatially close cysteine residues. Raw3-IP exhibits a characteristic surface charge pattern with a positively charged, a hydrophobic, and a negatively charged region. The RCK4 inactivation peptide (RCK4-IP) shows a similar spatial distribution of charged and uncharged regions, but is more flexible and less ordered in its amino-terminal part.

PubMed: 9000078
DOI: 10.1038/385272a0

Experimental method

SOLUTION NMR