TRPM5 Channel Binds Calcium-Binding Proteins Calmodulin and S100A1
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F22%3A00556398" target="_blank" >RIV/61388963:_____/22:00556398 - isvavai.cz</a>
Alternative codes found
RIV/00216208:11320/22:10441280 RIV/00216208:11130/22:10441280
Result on the web
<a href="https://doi.org/10.1021/acs.biochem.1c00647" target="_blank" >https://doi.org/10.1021/acs.biochem.1c00647</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1021/acs.biochem.1c00647" target="_blank" >10.1021/acs.biochem.1c00647</a>
Alternative languages
Result language
angličtina
Original language name
TRPM5 Channel Binds Calcium-Binding Proteins Calmodulin and S100A1
Original language description
Melastatin transient receptor potential (TRPM) channels belong to one of the most significant subgroups of the transient receptor potential (TRP) channel family. Here, we studied the TRPM5 member, the receptor exposed to calcium-mediated activation, resulting in taste transduction. It is known that most TRP channels are highly modulated through interactions with extracellular and intracellular agents. The binding sites for these ligands are usually located at the intracellular N- and C-termini of the TRP channels, and they can demonstrate the character of an intrinsically disordered protein (IDP), which allows such a region to bind various types of molecules. We explored the N-termini of TRPM5 and found the intracellular regions for calcium-binding proteins (CBPs) the calmodulin (CaM) and calcium-binding protein S1 (S100A1) by in vitro binding assays. Furthermore, molecular docking and molecular dynamics simulations (MDs) of the discovered complexes confirmed their known common binding interface patterns and the uniqueness of the basic residues present in the TRPM binding regions for CaM/S100A1.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology
Result continuities
Project
<a href="/en/project/GA19-04099S" target="_blank" >GA19-04099S: Role of nucleophosmin interactome in acute myeloid leukemia with mutated NPM</a><br>
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2022
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Biochemistry
ISSN
0006-2960
e-ISSN
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Volume of the periodical
61
Issue of the periodical within the volume
6
Country of publishing house
US - UNITED STATES
Number of pages
11
Pages from-to
413-423
UT code for WoS article
000771920200002
EID of the result in the Scopus database
2-s2.0-85126069353