1BYW

STRUCTURE OF THE N-TERMINAL DOMAIN OF THE HUMAN-ERG POTASSIUM CHANNEL

Summary for 1BYW

• Entry DOI: 10.2210/pdb1byw/pdb
• Descriptor: PROTEIN (HUMAN ERG POTASSIUM CHANNEL) (2 entities in total)
• Functional Keywords: pas domain, potassium channel domain, membrane protein
• Biological source: Homo sapiens (human)
• Cellular location: Cell membrane ; Multi- pass membrane protein : Q12809
• Total number of polymer chains: 1
• Total formula weight: 12346.40

Authors

Cabral, J.H.M.,Lee, A.,Mackinnon, R. (deposition date: 1998-10-15, release date: 1998-12-16, Last modification date: 2024-02-07)

Primary citation

Cabral, J.H.M.,Lee, A.,Cohen, S.L.,Chait, B.T.,Li, M.,Mackinnon, R.
Crystal Structure and Functional Analysis of the Herg Potassium Channel N-Terminus: A Eukaryotic Pas Domain
Cell(Cambridge,Mass.), 95:649-655, 1998

PubMed Abstract: The HERG voltage-dependent K+ channel plays a role in cardiac electrical excitability, and when defective, it underlies one form of the long QT syndrome. We have determined the crystal structure of the HERG K+ channel N-terminal domain and studied its role as a modifier of gating using electrophysiological methods. The domain is similar in structure to a bacterial light sensor photoactive yellow protein and provides the first three-dimensional model of a eukaryotic PAS domain. Scanning mutagenesis of the domain surface has allowed the identification of a hydrophobic "hot spot" forming a putative interface with the body of the K+ channel to which it tightly binds. The presence of the domain attached to the channel slows the rate of deactivation. Given the roles of PAS domains in biology, we propose that the HERG N-terminal domain has a regulatory function.

PubMed: 9845367
DOI: 10.1016/S0092-8674(00)81635-9

Experimental method

X-RAY DIFFRACTION (2.6 Å)