PDBsum entry 2n7g

Membrane protein

PDB id: 2n7g

Contents

Protein chain

131 a.a.

PDB id:

2n7g

Name:

Membrane protein

Title:

Structure of the cyclic nucleotide-binding homology domain of the herg channel

Structure:

Potassium voltage-gated channel subfamily h member 2. Chain: a. Fragment: unp residues 734-869. Synonym: eag homolog, ether-a-go-go-related gene potassium channel 1, erg-1, eag-related protein 1, ether-a-go-go-related protein 1, h-erg, herg-1, herg1, voltage-gated potassium channel subunit kv11.1. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: kcnh2, erg, erg1, herg. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

20 models

Authors:

Y.Li,H.Ng,Q.Li,C.Kang

Key ref:

Y.Li et al. (2016). Structure of the Cyclic Nucleotide-Binding Homology Domain of the hERG Channel and Its Insight into Type 2 Long QT Syndrome. Sci Rep, 6, 23712. PubMed id: 27025590 DOI: 10.1038/srep23712

Date:

10-Sep-15 Release date: 18-May-16

Protein chain

Q12809  (KCNH2_HUMAN) -  Potassium voltage-gated channel subfamily H member 2 from Homo sapiens

Seq: 1159 a.a.

Struc: 131 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1038/srep23712

Sci Rep 6:23712 (2016)

PubMed id: 27025590

Structure of the Cyclic Nucleotide-Binding Homology Domain of the hERG Channel and Its Insight into Type 2 Long QT Syndrome.

Y.Li, H.Q.Ng, Q.Li, C.Kang.

ABSTRACT

The human ether-à-go-go related gene (hERG) channel is crucial for the cardiac action potential by contributing to the fast delayed-rectifier potassium current. Mutations in the hERG channel result in type 2 long QT syndrome (LQT2). The hERG channel contains a cyclic nucleotide-binding homology domain (CNBHD) and this domain is required for the channel gating though molecular interactions with the eag domain. Here we present solution structure of the CNBHD of the hERG channel. The structural study reveals that the CNBHD adopts a similar fold to other KCNH channels. It is self-liganded and it contains a short β-strand that blocks the nucleotide-binding pocket in the β-roll. Folding of LQT2-related mutations in this domain was shown to be affected by point mutation. Mutations in this domain can cause protein aggregation in E. coli cells or induce conformational changes. One mutant-R752W showed obvious chemical shift perturbation compared with the wild-type, but it still binds to the eag domain. The helix region from the N-terminal cap domain of the hERG channel showed unspecific interactions with the CNBHD.