TRPM7 N-terminal region forms complexes with calcium binding proteins CaM and S100A1
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F21%3A00549345" target="_blank" >RIV/61388963:_____/21:00549345 - isvavai.cz</a>
Alternative codes found
RIV/00216208:11320/21:10434931 RIV/00216208:11130/21:10434931
Result on the web
<a href="https://doi.org/10.1016/j.heliyon.2021.e08490" target="_blank" >https://doi.org/10.1016/j.heliyon.2021.e08490</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.heliyon.2021.e08490" target="_blank" >10.1016/j.heliyon.2021.e08490</a>
Alternative languages
Result language
angličtina
Original language name
TRPM7 N-terminal region forms complexes with calcium binding proteins CaM and S100A1
Original language description
Transient receptor potential melastatin 7 (TRPM7) represents melastatin TRP channel with two significant functions, cation permeability and kinase activity. TRPM7 is widely expressed among tissues and is therefore involved in a variety of cellular functions representing mainly Mg2+ homeostasis, cellular Ca2+ flickering, and the regulation of DNA transcription by a cleaved kinase domain translocated to the nucleus. TRPM7 participates in several important biological processes in the nervous and cardiovascular systems. Together with the necessary function of the TRPM7 in these tissues and its recently analyzed overall structure, this channel requires further studies leading to the development of potential therapeutic targets. Here we present the first study investigating the N-termini of TRPM7 with binding regions for important intracellular modulators calmodulin (CaM) and calcium-binding protein S1 (S100A1) using in vitro and in silico approaches. Molecular simulations of the discovered complexes reveal their potential binding interfaces with common interaction patterns and the important role of basic residues present in the N-terminal binding region of TRPM.
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
2021
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Heliyon
ISSN
2405-8440
e-ISSN
2405-8440
Volume of the periodical
7
Issue of the periodical within the volume
12
Country of publishing house
GB - UNITED KINGDOM
Number of pages
7
Pages from-to
e08490
UT code for WoS article
000748925400017
EID of the result in the Scopus database
2-s2.0-85120421898