TY  - JOUR
AU  - Schünke, Sven
AU  - Stoldt, Matthias
TI  - Structural snapshot of cyclic nucleotide binding domains from cyclic nucleotide-sensitive ion channels.
JO  - Biological chemistry
VL  - 394
IS  - 11
SN  - 1437-4315
CY  - Berlin [u.a.]
PB  - de Gruyter
M1  - FZJ-2015-04392
SP  - 1439–1451
PY  - 2013
AB  - Cyclic nucleotide-binding domains (CNBDs) that are present in various channel proteins play crucial roles in signal amplification cascades. Although atomic resolution structures of some of those CNBDs are available, the detailed mechanism by which they confer cyclic nucleotide-binding to the ion channel pore remains poorly understood. In this review, we describe structural insights about cyclic nucleotide-binding-induced conformational changes in CNBDs and their potential coupling with channel gating.
KW  - Calcium Channels (NLM Chemicals)
KW  - Cyclic Nucleotide-Gated Cation Channels (NLM Chemicals)
KW  - Ligands (NLM Chemicals)
KW  - Potassium Channels, Voltage-Gated (NLM Chemicals)
KW  - Sodium Channels (NLM Chemicals)
KW  - Cyclic AMP (NLM Chemicals)
LB  - PUB:(DE-HGF)36 ; PUB:(DE-HGF)16
C6  - pmid:24021595
UR  - <Go to ISI:>//WOS:000325717100008
DO  - DOI:10.1515/hsz-2013-0228
UR  - https://juser.fz-juelich.de/record/202103
ER  -