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• W2034179468 startingPage "475" @default.
• W2034179468 abstract "There is controversy over whether Ca2+ binds to the BKCa channel's intracellular domain or its integral-membrane domain and over whether or not mutations that reduce the channel's Ca2+ sensitivity act at the point of Ca2+ coordination. One region in the intracellular domain that has been implicated in Ca2+ sensing is the “Ca2+ bowl”. This region contains many acidic residues, and large Ca2+-bowl mutations eliminate Ca2+ sensing through what appears to be one type of high-affinity Ca2+-binding site. Here, through site-directed mutagenesis we have mapped the residues in the Ca2+ bowl that are most important for Ca2+ sensing. We find acidic residues, D898 and D900, to be essential, and we find them essential as well for Ca2+ binding to a fusion protein that contains a portion of the BKCa channel's intracellular domain. Thus, much of our data supports the conclusion that Ca2+ binds to the BKCa channel's intracellular domain, and they define the Ca2+ bowl's essential Ca2+-sensing motif. Overall, however, we have found that the relationship between mutations that disrupt Ca2+ sensing and those that disrupt Ca2+ binding is not as strong as we had expected, a result that raises the possibility that, when examined by gel-overlay, the Ca2+ bowl may be in a nonnative conformation." @default.
• W2034179468 created "2016-06-24" @default.
• W2034179468 creator A5002829707 @default.
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• W2034179468 date "2004-04-26" @default.
• W2034179468 modified "2023-09-23" @default.
• W2034179468 title "Mapping the BKCa Channel's “Ca2+ Bowl”" @default.
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• W2034179468 doi "https://doi.org/10.1085/jgp.200409052" @default.
• W2034179468 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2234491" @default.
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