1UJL

Solution Structure of the HERG K+ channel S5-P extracellular linker

Summary for 1UJL

• Entry DOI: 10.2210/pdb1ujl/pdb
• NMR Information: BMRB: 5922
• Descriptor: Potassium voltage-gated channel subfamily H member 2 (1 entity in total)
• Functional Keywords: two helices, amphiphatic helix, membrane protein
• Cellular location: Membrane; Multi-pass membrane protein: Q12809
• Total number of polymer chains: 1
• Total formula weight: 4589.13

Authors

Torres, A.M.,Bansal, P.S.,Sunde, M.,Clarke, C.E.,Bursill, J.A.,Smith, D.J.,Bauskin, A.,Breit, S.N.,Campbell, T.J.,Alewood, P.F.,Kuchel, P.W.,Vandenberg, J.I. (deposition date: 2003-08-05, release date: 2003-11-04, Last modification date: 2023-12-27)

Primary citation

Torres, A.M.,Bansal, P.S.,Sunde, M.,Clarke, C.E.,Bursill, J.A.,Smith, D.J.,Bauskin, A.,Breit, S.N.,Campbell, T.J.,Alewood, P.F.,Kuchel, P.W.,Vandenberg, J.I.
Structure of the HERG K+ channel S5P extracellular linker: role of an amphipathic alpha-helix in C-type inactivation.
J.Biol.Chem., 278:42136-42148, 2003

PubMed Abstract: The HERG K+ channel has very unusual kinetic behaviour that includes slow activation but rapid inactivation. These features are critical for normal cardiac repolarisation as well as in preventing lethal ventricular arrhythmias. Extensive mutagenesis of the HERG K+ channel has allowed identification of which regions of the channel are important for the unusual kinetic behaviour of the channel. Furthermore, structural studies on scorpion toxins that potently inhibit HERG are beginning to provide clues as to the structural differences between HERG and other voltage-gated K+ channels.

PubMed: 13680209
DOI: 10.1074/jbc.M212824200

Experimental method

SOLUTION NMR