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PtdIns(4,5)P-2 interacts with CaM binding domains on TRPM3 N-terminus
- 1.0388283 - FGÚ 2013 RIV US eng J - Journal Article
Holendová, Blanka - Gryčová, Lenka - Jirků, Michaela - Teisinger, Jan
PtdIns(4,5)P-2 interacts with CaM binding domains on TRPM3 N-terminus.
Channels. Roč. 6, č. 6 (2012), s. 479-482. ISSN 1933-6950. E-ISSN 1933-6969
R&D Projects: GA ČR(CZ) GAP301/10/1159; GA ČR(CZ) GPP205/10/P308; GA ČR(CZ) GD305/03/H148
Institutional research plan: CEZ:AV0Z50110509
Keywords : TRPM3 * calmodulin * S100A1 * PIP2 * surface plasmon resonance * fluorescence anisotropy
Subject RIV: BO - Biophysics
Impact factor: 2.159, year: 2012
The transient receptor potential channel TRPM3 belongs to the melastatin TRP subfamily. In our study we identified two independent calmodulin/S100A1 binding sites on the N-terminus of TRPM3 (A35-H124 and H291-G382), which contain conserved hydrophobic as well as positively charged residues in specific positions. Moreover, our results suggest that another very important TRP channel activity modulator, PtdIns(4,5)P2, interacts with the calmodulin/S100A1 binding sites on the TRPM3 N-terminus with high affinity
Permanent Link: http://hdl.handle.net/11104/0217124
Number of the records: 1