Source:http://linkedlifedata.com/resource/pubmed/id/18379773
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
2008-6-18
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pubmed:abstractText |
Three constructs are used for the analysis of biophysical properties of CNGA1 channels: the WT CNGA1 channel, a CNGA1 channel where all endogenous cysteines were removed (CNGA1cys-free) and a construct composed of two CNGA1 subunits connected by a small linker (CNGA1tandem). So far, it has been assumed, but not proven, that the molecular structure of these ionic channels is almost identical. The I/V relations, ionic selectivity to alkali monovalent cations, blockage by tetracaine and TMA+ were not significantly different. The cGMP dose response and blockage by TEA+ and Cd2+ were instead significantly different in CNGA1 and CNGA1cys-free channels, but not in CNGA1 and CNGA1tandem channels. Cd2+ blocked irreversibly the mutant channel A406C in the absence of cGMP. By contrast, Cd2+ did not block the mutant channel A406C in the CNGA1cys-free background (A406Ccys-free), but an irreversible and almost complete blockage was observed in the presence of the cross-linker M-4-M. Results obtained with different MTS cross-linkers and reagents suggest that the 3D structure of the CNGA1cys-free differs from that of the CNGA1 channel and that the distance between homologous residues at position 406 in CNGA1cys-free is longer than in the WT CNGA1 by several Angstroms.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0175-7571
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
37
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
947-59
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pubmed:meshHeading |
pubmed-meshheading:18379773-Amino Acid Sequence,
pubmed-meshheading:18379773-Animals,
pubmed-meshheading:18379773-Cells, Cultured,
pubmed-meshheading:18379773-Cyclic Nucleotide-Gated Cation Channels,
pubmed-meshheading:18379773-Ion Channel Gating,
pubmed-meshheading:18379773-Membrane Potentials,
pubmed-meshheading:18379773-Molecular Sequence Data,
pubmed-meshheading:18379773-Oocytes,
pubmed-meshheading:18379773-Structure-Activity Relationship,
pubmed-meshheading:18379773-Xenopus laevis
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pubmed:year |
2008
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pubmed:articleTitle |
A comparison of electrophysiological properties of the CNGA1, CNGA1tandem and CNGA1cys-free channels.
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pubmed:affiliation |
International School for Advanced Studies, via Beirut 2-4, 34014, Trieste, Italy.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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