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rdf:type |
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lifeskim:mentions |
umls-concept:C0022009,
umls-concept:C0205245,
umls-concept:C0439799,
umls-concept:C0439849,
umls-concept:C0443203,
umls-concept:C0445223,
umls-concept:C0449379,
umls-concept:C0596988,
umls-concept:C1325742,
umls-concept:C1552599,
umls-concept:C1704787
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pubmed:issue |
5085
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pubmed:dateCreated |
1992-12-17
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pubmed:abstractText |
The overall sequence similarity between the voltage-activated K+ channels and cyclic nucleotide-gated ion channels from retinal and olfactory neurons suggests that they arose from a common ancestor. On the basis of sequence comparisons, mutations were introduced into the pore of a voltage-activated K+ channel. These mutations confer the essential features of ion conduction in the cyclic nucleotide-gated ion channels; the mutant K+ channels display little selectivity among monovalent cations and are blocked by divalent cations. The property of K+ selectivity is related to the presence of two amino acids that are absent from the pore-forming region of the cyclic nucleotide-gated channels. These data demonstrate that very small differences in the primary structure of an ion channel can account for extreme functional diversity, and they suggest a possible connection between the pore-forming regions of K+, Ca2+, and cyclic nucleotide-gated ion channels.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0036-8075
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pubmed:author |
|
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pubmed:issnType |
Print
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pubmed:day |
13
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pubmed:volume |
258
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1152-5
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:1279807-Amino Acid Sequence,
pubmed-meshheading:1279807-Animals,
pubmed-meshheading:1279807-Calcium,
pubmed-meshheading:1279807-Cattle,
pubmed-meshheading:1279807-Cyclic AMP,
pubmed-meshheading:1279807-Cyclic GMP,
pubmed-meshheading:1279807-Drosophila,
pubmed-meshheading:1279807-Electric Conductivity,
pubmed-meshheading:1279807-Ion Channel Gating,
pubmed-meshheading:1279807-Ion Channels,
pubmed-meshheading:1279807-Magnesium,
pubmed-meshheading:1279807-Molecular Sequence Data,
pubmed-meshheading:1279807-Mutagenesis, Site-Directed,
pubmed-meshheading:1279807-Oocytes,
pubmed-meshheading:1279807-Plants,
pubmed-meshheading:1279807-Potassium Channels,
pubmed-meshheading:1279807-Retina,
pubmed-meshheading:1279807-Transfection,
pubmed-meshheading:1279807-Xenopus laevis
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pubmed:year |
1992
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pubmed:articleTitle |
A functional connection between the pores of distantly related ion channels as revealed by mutant K+ channels.
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pubmed:affiliation |
Department of Neurobiology, Harvard Medical School, Boston, MA 02115.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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