TRPM5 Channel Binds Calcium-Binding Proteins Calmodulin and S100A1

Kód výsledku v 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>

Nalezeny alternativní kódy

RIV/00216208:11320/22:10441280 RIV/00216208:11130/22:10441280

Výsledek na webu

<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>

Jazyk výsledku

angličtina

Název v původním jazyce

TRPM5 Channel Binds Calcium-Binding Proteins Calmodulin and S100A1

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

TRPM5 Channel Binds Calcium-Binding Proteins Calmodulin and S100A1

Popis výsledku anglicky

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.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

<a href="/cs/project/GA19-04099S" target="_blank" >GA19-04099S: Role interakční sítě nukleofosminu v akutní myeloidní leukémii s mutovaným NPM</a><br>

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2022

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Biochemistry

ISSN

0006-2960

e-ISSN

—

Svazek periodika

61

Číslo periodika v rámci svazku

6

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

11

Strana od-do

413-423

Kód UT WoS článku

000771920200002

EID výsledku v databázi Scopus

2-s2.0-85126069353