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001     202103
005     20210129220030.0
024 7 _ |a 10.1515/hsz-2013-0228
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024 7 _ |a pmid:24021595
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024 7 _ |a 1431-6730
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024 7 _ |a 1437-4315
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037 _ _ |a FZJ-2015-04392
041 _ _ |a eng
082 _ _ |a 540
100 1 _ |a Schünke, Sven
|0 P:(DE-Juel1)132020
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245 _ _ |a Structural snapshot of cyclic nucleotide binding domains from cyclic nucleotide-sensitive ion channels.
260 _ _ |a Berlin [u.a.]
|c 2013
|b de Gruyter
336 7 _ |a Output Types/Book Review
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336 7 _ |a Review
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520 _ _ |a 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.
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650 _ 7 |a Calcium Channels
|2 NLM Chemicals
650 _ 7 |a Cyclic Nucleotide-Gated Cation Channels
|2 NLM Chemicals
650 _ 7 |a Ligands
|2 NLM Chemicals
650 _ 7 |a Potassium Channels, Voltage-Gated
|2 NLM Chemicals
650 _ 7 |a Sodium Channels
|2 NLM Chemicals
650 _ 7 |a Cyclic AMP
|0 E0399OZS9N
|2 NLM Chemicals
700 1 _ |a Stoldt, Matthias
|0 P:(DE-Juel1)132023
|b 1
|e Corresponding Author
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773 _ _ |a 10.1515/hsz-2013-0228
|g Vol. 394, no. 11
|0 PERI:(DE-600)1466062-3
|n 11
|p 1439–1451
|t Biological chemistry
|v 394
|y 2013
|x 1437-4315
856 4 _ |y OpenAccess
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