Title : Allosteric interactions required for high-affinity binding of dihydropyridine antagonists to Ca(V)1.1 Channels are modulated by calcium in the pore.

Pub. Date : 2006 Aug

PMID : 16675661






2 Functional Relationships(s)
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1 Analysis of mutations of amino acid residues adjacent to the selectivity filter led to identification of Phe-1013 and Tyr-1021, whose mutation causes substantial changes in DHP binding. Phenylalanine dihydropyrimidinase Homo sapiens
2 We propose that DHP binding stabilizes a nonconducting state containing a single Ca(2+) ion in the pore through which Phe-1013 and Tyr-1021 are energetically coupled. Phenylalanine dihydropyrimidinase Homo sapiens