5KHK

HCN2 CNBD in complex with 2-aminopurine riboside-3', 5'-cyclic monophosphate (2-NH2-cPuMP)

5KHK の概要

• エントリーDOI: 10.2210/pdb5khk/pdb
• 関連するPDBエントリー: 5KHG 5KHH 5KHI 5KHJ
• 分子名称: Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2, 2-Aminopurine riboside-3',5'-cyclic monophosphate (3 entities in total)
• 機能のキーワード: protein-ligand complex, cycilc nucleotide binding domain, ion transport, transport protein
• 由来する生物種: Mus musculus (Mouse)
• 細胞内の位置: Cell membrane ; Multi-pass membrane protein : O88703
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 24212.54

構造登録者

Ng, L.C.T.,Putrenko, I.,Baronas, V.,Van Petegem, F.,Accili, E.A. (登録日: 2016-06-14, 公開日: 2016-09-14, 最終更新日: 2023-09-27)

主引用文献

Ng, L.C.,Putrenko, I.,Baronas, V.,Van Petegem, F.,Accili, E.A.
Cyclic Purine and Pyrimidine Nucleotides Bind to the HCN2 Ion Channel and Variably Promote C-Terminal Domain Interactions and Opening.
Structure, 24:1629-1642, 2016

PubMed Abstract: Cyclic AMP is thought to facilitate the opening of the HCN2 channel by binding to a C-terminal domain and promoting or inhibiting interactions between subunits. Here, we correlated the ability of cyclic nucleotides to promote interactions of isolated HCN2 C-terminal domains in solution with their ability to facilitate channel opening. Cyclic IMP, a cyclic purine nucleotide, and cCMP, a cyclic pyrimidine nucleotide, bind to a C-terminal domain containing the cyclic nucleotide-binding domain but, in contrast to other cyclic nucleotides examined, fail to promote its oligomerization, and produce only modest facilitation of opening of the full-length channel. Comparisons between ligand bound structures identify a region between the sixth and seventh β strands and the distal C helix as important for facilitation and tight binding. We propose that promotion of interactions between the C-terminal domains by a given ligand contribute to its ability to facilitate opening of the full-length channel.

PubMed: 27568927
DOI: 10.1016/j.str.2016.06.024

実験手法

X-RAY DIFFRACTION (2.07 Å)