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Related Experiment Videos

Toward linking structure with function in ATP-sensitive K+ channels.

Joseph Bryan1, Wanda H Vila-Carriles, Guiling Zhao

  • 1Department of Molecular and Cellular Biology, Baylor College of Medicine, Houston, TX 77030, USA. jbryan@bcm.tmc.edu

Diabetes
|November 25, 2004
PubMed
Summary
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Structural insights into ATP-sensitive K+ channels (KATP channels) reveal how sulfonylurea receptor (SUR) components activate KIR6.0. The SUR1 binding pocket for glibenclamide is bipartite, influencing channel gating.

Area of Science:

  • Molecular biology
  • Structural biology
  • Biophysics

Background:

  • ATP-sensitive K+ channels (KATP channels) are crucial for cellular energy homeostasis.
  • Understanding the structure of KATP channels (KIR6.0/SUR) is key to elucidating their function.
  • Advances in structural biology of inward rectifiers and ABC transporters inform KATP channel architecture.

Purpose of the Study:

  • To provide novel insight into the architecture of ATP-sensitive K+ channels (KATP channels).
  • To model the structure of the K(IR) pore and the MDR-like core of sulfonylurea receptor (SUR)-1.
  • To define the glibenclamide/sulfonylurea binding pocket in SUR1.

Main Methods:

  • Modeling the K(IR) pore based on bacterial K+ channels.
  • Utilizing the lipid-A exporter MsbA as a template for the SUR-1 core.

Related Experiment Videos

  • Homology modeling of the SUR1 core to identify drug binding sites.

    • Main Results:

    • The NH2-terminal TMD0 of SURs binds to and activates KIR6.0.
    • The cytoplasmic L0 linker connects the SUR core to the KIR6.2/TMD0 complex and controls gating.
    • The glibenclamide/sulfonylurea binding pocket in SUR1 is bipartite, with distinct regions interacting with different parts of the drug.

    Conclusions:

    • The structural understanding of KATP channels reveals the roles of SUR components in channel activation and gating.
    • The bipartite nature of the SUR1 binding pocket explains the selectivity of glibenclamide.
    • These findings advance the comprehension of KATP channel mechanisms and drug interactions.