Characterization of the part of N-terminal PIP2 binding site of the TRPM1 channel
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F15%3A10315319" target="_blank" >RIV/00216208:11310/15:10315319 - isvavai.cz</a>
Alternative codes found
RIV/67985823:_____/15:00454381 RIV/61388971:_____/15:00454381 RIV/61388963:_____/15:00454381 RIV/00216208:11120/15:43910370 and 2 more
Result on the web
<a href="http://dx.doi.org/10.1016/j.bpc.2015.10.005" target="_blank" >http://dx.doi.org/10.1016/j.bpc.2015.10.005</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.bpc.2015.10.005" target="_blank" >10.1016/j.bpc.2015.10.005</a>
Alternative languages
Result language
angličtina
Original language name
Characterization of the part of N-terminal PIP2 binding site of the TRPM1 channel
Original language description
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 1(464 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.
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
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Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2015
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Biophysical Chemistry
ISSN
0301-4622
e-ISSN
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Volume of the periodical
207
Issue of the periodical within the volume
December
Country of publishing house
NL - THE KINGDOM OF THE NETHERLANDS
Number of pages
8
Pages from-to
135-142
UT code for WoS article
000366442800016
EID of the result in the Scopus database
2-s2.0-84946236868