Pub. Date : 2004 Sep
PMID : 15314069
4 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | The molecular basis for Ca(2+)/CaM inhibition of rod CNG channels has been proposed to involve the binding of Ca(2+)/CaM to a site in the NH(2)-terminal region of the CNGB1 subunit, which disrupts an interaction between the NH(2)-terminal region of CNGB1 and the COOH-terminal region of CNGA1. | cafestol palmitate | cyclic nucleotide gated channel subunit alpha 1 | Homo sapiens |
| 2 | The molecular basis for Ca(2+)/CaM inhibition of rod CNG channels has been proposed to involve the binding of Ca(2+)/CaM to a site in the NH(2)-terminal region of the CNGB1 subunit, which disrupts an interaction between the NH(2)-terminal region of CNGB1 and the COOH-terminal region of CNGA1. | cafestol palmitate | cyclic nucleotide gated channel subunit alpha 1 | Homo sapiens |
| 3 | Here, we test this mechanism for Ca(2+)/CaM-dependent inhibition of CNGA1/CNGB1 channels by simultaneously monitoring protein interactions with fluorescence spectroscopy and channel function with patch-clamp recording. | cafestol palmitate | cyclic nucleotide gated channel subunit alpha 1 | Homo sapiens |
| 4 | Further, we show that the NH(2)- and COOH-terminal regions of CNGB1 and CNGA1 subunits, respectively, are in close proximity, and that Ca(2+)/CaM binding causes a relative rearrangement or separation of these regions. | cafestol palmitate | cyclic nucleotide gated channel subunit alpha 1 | Homo sapiens |