Review/Journal Article

FZJ-2015-04392

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Structural snapshot of cyclic nucleotide binding domains from cyclic nucleotide-sensitive ion channels.

Schünke, S. ; Stoldt, M. (Corresponding Author)FZJ*

2013
de Gruyter Berlin [u.a.]

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Please use a persistent id in citations: http://hdl.handle.net/2128/18350  doi:10.1515/hsz-2013-0228

Abstract: 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.

Keyword(s): Calcium Channels ; Cyclic Nucleotide-Gated Cation Channels ; Ligands ; Potassium Channels, Voltage-Gated ; Sodium Channels ; Cyclic AMP

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Contributing Institute(s):

1. Strukturbiochemie (ICS-6)

Research Program(s):

1. 452 - Structural Biology (POF2-452) (POF2-452)

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Database coverage:
; ; BIOSIS Previews ; Current Contents - Life Sciences ; IF < 5 ; JCR ; NCBI Molecular Biology Database ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection

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