2PTM

Structure and rearrangements in the carboxy-terminal region of SpIH channels

2PTM の概要

• エントリーDOI: 10.2210/pdb2ptm/pdb
• 分子名称: Hyperpolarization-activated (Ih) channel, COBALT HEXAMMINE(III), ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: ion channel, cyclic nucleotide binding domain, c-linker, camp, cgmp, sphcn1, hcn, transport protein
• 由来する生物種: Strongylocentrotus purpuratus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 23782.90

構造登録者

Flynn, G.E.,Black, K.D.,Islas, L.D.,Sankaran, B.,Zagotta, W.N. (登録日: 2007-05-08, 公開日: 2007-06-19, 最終更新日: 2023-08-30)

主引用文献

Flynn, G.E.,Black, K.D.,Islas, L.D.,Sankaran, B.,Zagotta, W.N.
Structure and rearrangements in the carboxy-terminal region of SpIH channels.
Structure, 15:671-682, 2007

PubMed Abstract: Hyperpolarization-activated cyclic nucleotide-modulated (HCN) ion channels regulate the spontaneous firing activity and electrical excitability of many cardiac and neuronal cells. The modulation of HCN channel opening by the direct binding of cAMP underlies many physiological processes such as the autonomic regulation of the heart rate. Here we use a combination of X-ray crystallography and electrophysiology to study the allosteric mechanism for cAMP modulation of HCN channels. SpIH is an invertebrate HCN channel that is activated fully by cAMP, but only partially by cGMP. We exploited the partial agonist action of cGMP on SpIH to reveal the molecular mechanism for cGMP specificity of many cyclic nucleotide-regulated enzymes. Our results also elaborate a mechanism for the allosteric conformational change in the cyclic nucleotide-binding domain and a mechanism for partial agonist action. These mechanisms will likely extend to other cyclic nucleotide-regulated channels and enzymes as well.

PubMed: 17562314
DOI: 10.1016/j.str.2007.04.008

実験手法

X-RAY DIFFRACTION (1.93 Å)