Does the KdpA subunit from the high affinity K(+)-translocating P-type KDP-ATPase have a structure similar to that of K(+) channels?

Durell, S R; Bakker, E P; Guy, H R

Durell, S R; Bakker, E P; Guy, H R.

Affiliation

Durell SR; Laboratory of Experimental Biology, Division of Basic Sciences, National Cancer Institute, National Institutes of Health, 9000 Rockville Pike, Bethesda, Maryland 20892-5677, USA.

Biophys J ; 78(1): 188-99, 2000 Jan.

Article in En | MEDLINE | ID: mdl-10620285

Subject(s)

Adenosine Triphosphatases/chemistry; Carrier Proteins/chemistry; Cation Transport Proteins; Escherichia coli Proteins; Potassium Channels/chemistry; Adenosine Triphosphatases/metabolism; Amino Acid Sequence; Bacterial Proteins/chemistry; Carrier Proteins/metabolism; Cell Membrane/ultrastructure; Conserved Sequence; Databases as Topic; Evolution, Molecular; Macromolecular Substances; Models, Molecular; Molecular Sequence Data; Peptide Library; Potassium/metabolism; Protein Structure, Quaternary; Protein Structure, Secondary; Sequence Alignment; Sequence Homology, Amino Acid

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Potassium Channels / Carrier Proteins / Adenosine Triphosphatases / Escherichia coli Proteins / Cation Transport Proteins Language: En Journal: Biophys J Year: 2000 Document type: Article Affiliation country: United States Country of publication: United States

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