scholarly journals Solution structure of the Mesorhizobium loti K1 channel cyclic nucleotide‐binding domain in complex with cAMP

EMBO Reports ◽  
2009 ◽  
Vol 10 (7) ◽  
pp. 729-735 ◽  
Author(s):  
Sven Schünke ◽  
Matthias Stoldt ◽  
Kerstin Novak ◽  
U Benjamin Kaupp ◽  
Dieter Willbold
Keyword(s):  
Cyclic Nucleotide ◽  
Solution Structure ◽  
Nucleotide Binding ◽  
Binding Domain ◽  
Nucleotide Binding Domain ◽  
Mesorhizobium Loti ◽  
Cyclic Nucleotide Binding ◽  
Cyclic Nucleotide Binding Domain

scholarly journals Allosteric signaling in C-linker and cyclic nucleotide-binding domain of HCN2 channels

2021 ◽  
Author(s):  
Christopher Pfleger ◽  
Jana Kusch ◽  
Mahesh Kondapuram ◽  
Tina Schwabe ◽  
Christian Sattler ◽  
...  
Keyword(s):  
Cyclic Nucleotide ◽  
Nucleotide Binding ◽  
Binding Domain ◽  
Nucleotide Binding Domain ◽  
Cyclic Nucleotide Binding ◽  
Cyclic Nucleotide Binding Domain

scholarly journals Structural and Energetic Analysis of Activation by a Cyclic Nucleotide Binding Domain

2008 ◽  
Vol 381 (3) ◽  
pp. 655-669 ◽  
Author(s):  
Stephen L. Altieri ◽  
Gina M. Clayton ◽  
William R. Silverman ◽  
Adrian O. Olivares ◽  
Enrique M. De La Cruz ◽  
...  
Keyword(s):  
Cyclic Nucleotide ◽  
Nucleotide Binding ◽  
Binding Domain ◽  
Nucleotide Binding Domain ◽  
Cyclic Nucleotide Binding ◽  
Energetic Analysis ◽  
Cyclic Nucleotide Binding Domain

scholarly journals A Na + /H + Exchanger Regulated by an S4 Voltage-Sensing Domain and a Cyclic Nucleotide-Binding Domain

2017 ◽  
Vol 112 (3) ◽  
pp. 335a-336a
Author(s):  
Reinhard Seifert ◽  
Florian Windler ◽  
Wolfgang Bönigk ◽  
Heinz-Gerd Körschen ◽  
U. Benjamin Kaupp
Keyword(s):  
Cyclic Nucleotide ◽  
Nucleotide Binding ◽  
Binding Domain ◽  
Nucleotide Binding Domain ◽  
Voltage Sensing ◽  
Cyclic Nucleotide Binding ◽  
Voltage Sensing Domain ◽  
Cyclic Nucleotide Binding Domain

scholarly journals FRET‐based binding assay between a fluorescent cAMP analogue and a cyclic nucleotide‐binding domain tagged with a CFP

FEBS Letters ◽  
2017 ◽  
Vol 591 (18) ◽  
pp. 2869-2878 ◽  
Author(s):  
Francisco Romero ◽  
Carmen Santana‐Calvo ◽  
Yoloxochitl Sánchez‐Guevara ◽  
Takuya Nishigaki
Keyword(s):  
Cyclic Nucleotide ◽  
Binding Assay ◽  
Nucleotide Binding ◽  
Binding Domain ◽  
Nucleotide Binding Domain ◽  
Cyclic Nucleotide Binding ◽  
Camp Analogue ◽  
Cyclic Nucleotide Binding Domain

scholarly journals Structural and Biochemical Characterization of a Cyclic Nucleotide Binding Domain from the EAG Family

2012 ◽  
Vol 102 (3) ◽  
pp. 330a
Author(s):  
Maria J. Marques Carvalho ◽  
Ricardo S. Vieira Pires ◽  
Guillaume Gabant ◽  
Martine Cadene ◽  
João H. Morais Cabral
Keyword(s):  
Cyclic Nucleotide ◽  
Biochemical Characterization ◽  
Nucleotide Binding ◽  
Binding Domain ◽  
Nucleotide Binding Domain ◽  
Cyclic Nucleotide Binding ◽  
Cyclic Nucleotide Binding Domain

Cyclic-nucleotide- and Ca2+/calmodulin-regulated channels in plants: targets for manipulating heavy-metal tolerance, and possible physiological roles

2000 ◽  
Vol 28 (4) ◽  
pp. 471-475 ◽  
Author(s):  
T. Arazi ◽  
B. Kaplan ◽  
R. Sunkar ◽  
H. Fromm
Keyword(s):  
Heavy Metal ◽  
Transgenic Plants ◽  
Cyclic Nucleotide ◽  
Metal Tolerance ◽  
Heavy Metal Tolerance ◽  
Nucleotide Binding ◽  
Binding Domain ◽  
Nucleotide Binding Domain ◽  
Cyclic Nucleotide Binding ◽  
Cyclic Nucleotide Binding Domain

Recently we discovered a tobacco protein (designated NtCBP4) that modulates heavy-metal tolerance in transgenic plants. Structurally, NtCBP4 is similar to mammalian cyclic-nucleotide-gated non-selective cation channels containing six putative transmembrane domains, a predicted pore region, a conserved cyclic-nucleotide-binding domain, and a high-affinity calmodulin-binding site that coincides with its cyclic-nucleotide-binding domain. Transgenic tobacco expressing the plasma-membrane-localized NtCBP4 exhibit improved tolerance to Ni2+ and hypersensitivity to Pb2+, which are associated with a decreased accumulation of Ni2+ and an enhanced accumulation of Pb2+ respectively. Transgenic plants expressing a truncated version of NtCBP4, from which regulatory domains had been removed, have a different phenotype. Here we describe our approach to studying the involvement of NtCBP4 in heavy-metal tolerance and to elucidate its physiological role.

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