2MHF

Solution structure of the cyclic-nucleotide binding homology domain of a KCNH channel

2MHF の概要

• エントリーDOI: 10.2210/pdb2mhf/pdb
• NMR情報: BMRB: 19621
• 分子名称: Uncharacterized protein (1 entity in total)
• 機能のキーワード: kcnh, dynamics, ion channel, nucleotide binding domain, transport protein
• 由来する生物種: Danio rerio (leopard danio, zebra danio, zebra fish)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16182.66

構造登録者

Li, Q.,Ng, H. (登録日: 2013-11-21, 公開日: 2014-04-02, 最終更新日: 2024-05-15)

主引用文献

Li, Q.,Ng, H.Q.,Yoon, H.S.,Kang, C.
Solution structure of the cyclic-nucleotide binding homology domain of a KCNH channel.
J.Struct.Biol., 186:68-74, 2014

PubMed Abstract: The carboxy-terminal region of the KCNH family of potassium channels contains a cyclic-nucleotide binding homology domain (CNBHD) that is important for channel gating and trafficking. The solution structure of the CNBHD of the KCNH potassium of zebrafish was determined using solution NMR spectroscopy. This domain exists as a monomer under solution conditions and adopts a similar fold to that determined by X-ray crystallography. The CNBHD does not bind cAMP because residue Y740 blocks the entry of cyclic-nucleotide to the binding pocket. Relaxation results show that the CNBHD is rigid except that some residues in the loop between β6 and β7 are flexible. Our results will be useful to understand the gating mechanism of KCNH family members through the CNBHD.

PubMed: 24632450
DOI: 10.1016/j.jsb.2014.03.008

実験手法

SOLUTION NMR