Structural snapshot of cyclic nucleotide binding domains from cyclic nucleotide-sensitive ion channels.
Structural snapshot of cyclic nucleotide binding domains from cyclic nucleotide-sensitive ion channels.
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 cha...
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Personal Name(s): | Schünke, Sven |
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Stoldt, Matthias (Corresponding Author) | |
Contributing Institute: |
Strukturbiochemie; ICS-6 |
Published in: | Biological chemistry, 394 (2013) 11, S. 1439–1451 |
Imprint: |
Berlin [u.a.]
de Gruyter
2013
|
PubMed ID: |
24021595 |
DOI: |
10.1515/hsz-2013-0228 |
Document Type: |
Review Journal Article |
Research Program: |
Structural Biology |
Subject (ZB): | |
Link: |
OpenAccess OpenAccess |
Publikationsportal JuSER |
Please use the identifier: http://dx.doi.org/10.1515/hsz-2013-0228 in citations.
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. |