Characterization of the part of N-terminal PIP2 binding site of the TRPM1 channel
Jazyk angličtina Země Nizozemsko Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
26544986
DOI
10.1016/j.bpc.2015.10.005
PII: S0301-4622(15)30068-5
Knihovny.cz E-zdroje
- Klíčová slova
- Binding site, Circular dichroism, FRET, PIP2, Surface plasmon resonance, TRPM1 channel,
- MeSH
- cirkulární dichroismus MeSH
- fosfatidylinositol-4,5-difosfát chemie metabolismus MeSH
- kationtové kanály TRPM chemie genetika metabolismus MeSH
- lidé MeSH
- povrchová plasmonová rezonance MeSH
- rekombinantní proteiny biosyntéza chemie izolace a purifikace MeSH
- sekundární struktura proteinů MeSH
- simulace molekulární dynamiky MeSH
- terciární struktura proteinů MeSH
- vazba proteinů MeSH
- vazebná místa MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- fosfatidylinositol-4,5-difosfát MeSH
- kationtové kanály TRPM MeSH
- rekombinantní proteiny MeSH
- TRPM1 protein, human MeSH Prohlížeč
Transient receptor potential melastatin-1 (TRPM1) is a calcium channel that is essential for the depolarization of photo-responsive retinal bipolar cells, but most of the physiological functions and cellular roles of this channel are still poorly understood. Most transient receptor potential (TRP) channels are typically regulated by intracellular proteins and other signaling molecules. Phosphatidylinositol-4,5 bisphosphate (PIP2), a minor phospholipid component of cell membranes, has previously been shown to directly bind TRP channels and to play a unique role in modulating receptor function. To characterize the binding of PIP2 as a potential regulator of TRPM1, we utilized biophysical methods and molecular modeling to study the interactions of PIP2 with an N-terminal fragment of TRPM1 (residues A451-N566). The basic N-terminal residue K464 of TRPM1 suggests that it is part of putative pleckstrin homology (PH) domain and is involved in the interactions with PIP2. This is the first report detailing the binding of PIP2 at the N-terminus of the TRPM1 receptor.
3rd Faculty of Medicine Charles University Prague 10000 Prague Czech Republic
Faculty of Science Palacky University 78341 Olomouc Czech Republic
Institute of Microbiology Academy of Sciences of the Czech Republic 14220 Prague Czech Republic
Institute of Physiology Academy of Sciences of the Czech Republic 14220 Prague Czech Republic
Citace poskytuje Crossref.org
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