Intramolecular interaction of SUR2 subtypes for intracellular ADP-induced differential control of KATP channels

Kenji Matsushita, Kengo Kinoshita, Tetsuro Matsuoka, Akikazu Fujita, Takashi Fujikado, Yasuo Tano, Haruki Nakamura, Yoshihisa Kurachi

Research output: Contribution to journalArticle

37 Citations (Scopus)

Abstract

ATP-sensitive K+ (KATP) channels are composed of sulfonylurea receptors (SURs) and inwardly rectifying Kir6.2-channels. The C-terminal 42 amino acid residues (C42) of SURs are responsible for ADP-induced differential activation of KATP channels in SUR-subtypes. By examining ADP-effect on KATP channels containing various chimeras of SUR2A and SUR2B, we identified a segment of 7 residues at central portion of C42 critical for this phenomenon. A 3-D structure model of the region containing the second nucleotide-binding domain (NBD2) of SUR and C42 was developed based on the structure of HisP, a nucleotide-binding protein forming the bacterial Histidine transporter complex. In the model, the polar and charged residues in the critical segment located within a distance that allows their electrostatic interaction with Arg1344 at the Walker-A loop of NBD2. Therefore, the interaction might be involved in the control of ADP-induced differential activation of SUR2-subtype KATP channels.

Original languageEnglish
Pages (from-to)554-561
Number of pages8
JournalCirculation research
Volume90
Issue number5
DOIs
Publication statusPublished - 2002 Mar 22

Keywords

  • Homology modeling
  • K channel
  • Nucleotide binding domain
  • Sulfonylurea receptor
  • Walker motif

ASJC Scopus subject areas

  • Physiology
  • Cardiology and Cardiovascular Medicine

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