PDBsum entry 5ywc

Membrane protein

PDB id: 5ywc

Contents

Protein chains

325 a.a.

1322 a.a.

Ligands

ADP ×12

Metals

_MG ×8

PDB id:

5ywc

Name:

Membrane protein

Title:

Structure of pancreatic atp-sensitive potassium channel bound with mg- adp (ctd class1 at 4.3a)

Structure:

Atp-sensitive inward rectifier potassium channel 11. Chain: a, c, e, g. Synonym: inward rectifier k(+) channel kir6.2,potassium channel, inwardly rectifying subfamily j member 11. Engineered: yes. Atp-binding cassette sub-family c member 8 isoform x2. Chain: b, d, f, h. Synonym: sur1. Engineered: yes

Source:

Mus musculus. Mouse. Organism_taxid: 10090. Gene: kcnj11. Expressed in: homo sapiens. Expression_system_taxid: 9606. Mesocricetus auratus. Golden hamster. Organism_taxid: 10036.

Authors:

L.Chen,J.X.Wu

Key ref:

J.X.Wu et al. (2018). Ligand binding and conformational changes of SUR1 subunit in pancreatic ATP-sensitive potassium channels. Protein Cell, 9, 553-567. PubMed id: 29594720 DOI: 10.1007/s13238-018-0530-y

Date:

29-Nov-17 Release date: 02-May-18

Protein chains

Q61743  (KCJ11_MOUSE) -  ATP-sensitive inward rectifier potassium channel 11 from Mus musculus

Seq: 390 a.a.

Struc: 325 a.a.

Protein chains

A0A1U7R319  (A0A1U7R319_MESAU) -  ATP-binding cassette sub-family C member 8 isoform X2 from Mesocricetus auratus

Seq: 1582 a.a.

Struc: 1322 a.a.

DOI no: 10.1007/s13238-018-0530-y

Protein Cell 9:553-567 (2018)

PubMed id: 29594720

Ligand binding and conformational changes of SUR1 subunit in pancreatic ATP-sensitive potassium channels.

J.X.Wu, D.Ding, M.Wang, Y.Kang, X.Zeng, L.Chen.

ABSTRACT

ATP-sensitive potassium channels (K_ATP) are energy sensors on the plasma membrane. By sensing the intracellular ADP/ATP ratio of β-cells, pancreatic K_ATP channels control insulin release and regulate metabolism at the whole body level. They are implicated in many metabolic disorders and diseases and are therefore important drug targets. Here, we present three structures of pancreatic K_ATP channels solved by cryo-electron microscopy (cryo-EM), at resolutions ranging from 4.1 to 4.5 Å. These structures depict the binding site of the antidiabetic drug glibenclamide, indicate how Kir6.2 (inward-rectifying potassium channel 6.2) N-terminus participates in the coupling between the peripheral SUR1 (sulfonylurea receptor 1) subunit and the central Kir6.2 channel, reveal the binding mode of activating nucleotides, and suggest the mechanism of how Mg-ADP binding on nucleotide binding domains (NBDs) drives a conformational change of the SUR1 subunit.