The characterization of a novel S100A1 binding site in the N-terminus of TRPM1
Jazyk angličtina Země Nizozemsko Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
27435061
DOI
10.1016/j.biocel.2016.07.014
PII: S1357-2725(16)30186-8
Knihovny.cz E-zdroje
- Klíčová slova
- Binding site, Calcium-binding protein S100A1, Circular dichroism, Molecular modeling, Steady-state fluorescence anisotropy, TRPM1 channel,
- MeSH
- hydrofobní a hydrofilní interakce MeSH
- kationtové kanály TRPM chemie metabolismus MeSH
- krysa rodu Rattus MeSH
- lidé MeSH
- proteinové domény MeSH
- proteiny S100 chemie metabolismus MeSH
- sekundární struktura proteinů MeSH
- sekvence aminokyselin MeSH
- simulace molekulového dockingu MeSH
- vápník metabolismus MeSH
- vazba proteinů MeSH
- vazebná místa MeSH
- zvířata MeSH
- Check Tag
- krysa rodu Rattus MeSH
- lidé MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- kationtové kanály TRPM MeSH
- proteiny S100 MeSH
- S100A1 protein MeSH Prohlížeč
- Trpm1 protein, rat MeSH Prohlížeč
- vápník MeSH
Transient receptor potential melastatin-1 channel (TRPM1) is an important mediator of calcium influx into the cell that is expressed in melanoma and ON-bipolar cells. Similar to other members of the TRP channel family, the intracellular N- and C- terminal domains of TRPM1 are expected to play important roles in the modulation of TRPM1 receptor function. Among the most commonly occurring modulators of TRP channels are the cytoplasmically expressed calcium binding proteins calmodulin and S100 calcium-binding protein A1 (S100A1), but the interaction of TRPM1 with S100A1 has not been described yet. Here, using a combination of biophysical and bioinformatics methods, we have determined that the N-terminal L242-E344 region of TRPM1 is a S100A1 binding domain. We show that formation of the TRPM1/S100A1 complex is calcium-dependent. Moreover, our structural model of the complex explained data obtained from fluorescence spectroscopy measurements revealing that the complex formation is facilitated through interactions of clusters positively charged (K271A, R273A, R274A) and hydrophobic (L263A, V270A, L276A) residues at the N-terminus of TRPM1. Taken together, our data suggest a molecular mechanism for the potential regulation of TRPM1 by S100A1.
Institute of Biotechnology Czech Academy of Sciences BIOCEV 25250 Vestec Czech Republic
Institute of Physiology Czech Academy of Sciences 14220 Prague Czech Republic
Citace poskytuje Crossref.org
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