rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
12
|
pubmed:dateCreated |
2001-12-17
|
pubmed:abstractText |
Due to the relative ease of obtaining their crystal structures, bacterial ion channels provide a unique opportunity to analyse structure and function of their eukaryotic homologues. This review describes prokaryotic channels whose structures have been determined. These channels are KcsA, a bacterial homologue of eukaryotic potassium channels, MscL, a bacterial mechanosensitive ion channel and ClC0, a prokaryotic homologue of the eukaryotic ClC family of anion-selective channels. General features of their structure and function are described with a special emphasis on the advantages that these channels offer for understanding the properties of their eukaryotic homologues. We present amino-acid sequences of eukaryotic proteins related in their primary sequences to bacterial mechanosensitive channels. The usefulness of bacterial mechanosensitive channels for the studies on general principles of mechanosensation is discussed.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Dec
|
pubmed:issn |
0265-9247
|
pubmed:author |
|
pubmed:copyrightInfo |
Copyright 2001 John Wiley & Sons, Inc.
|
pubmed:issnType |
Print
|
pubmed:volume |
23
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
1148-58
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:11746234-Amino Acid Sequence,
pubmed-meshheading:11746234-Animals,
pubmed-meshheading:11746234-Bacterial Proteins,
pubmed-meshheading:11746234-Chloride Channels,
pubmed-meshheading:11746234-Escherichia coli Proteins,
pubmed-meshheading:11746234-Eukaryotic Cells,
pubmed-meshheading:11746234-Humans,
pubmed-meshheading:11746234-Ion Channels,
pubmed-meshheading:11746234-Molecular Sequence Data,
pubmed-meshheading:11746234-Potassium Channels,
pubmed-meshheading:11746234-Protein Structure, Quaternary
|
pubmed:year |
2001
|
pubmed:articleTitle |
Bacterial ion channels and their eukaryotic homologues.
|
pubmed:affiliation |
Department of Cell Biology, Nencki Institute of Experimental Biology, Warsaw, Poland.
|
pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
|