Retinal Chromophore Environment in an Inward Light-Driven Proton Pump Studied by Solid-state NMR and Hydrogen-Bond Network Analysis DOI

Marie Pinto,

Maryam Saliminasab,

Andrew Harris

и другие.

Physical Chemistry Chemical Physics, Год журнала: 2024, Номер 26(36), С. 24090 - 24108

Опубликована: Янв. 1, 2024

The mechanism of inward proton transport in a microbial rhodopsin suggested by solid-state NMR spectroscopy and molecular dynamics simulations.

Язык: Английский

The complexity of G protein‐coupled receptor (GPCR) modulation and signalling DOI
Itziar Muneta‐Arrate, Antonella Di Pizio, Jana Selent

и другие.

British Journal of Pharmacology, Год журнала: 2025, Номер unknown

Опубликована: Май 9, 2025

Язык: Английский

Процитировано

0
Hydrogen-Bonding and Hydrophobic Interaction Networks as Structural Determinants of Microbial Rhodopsin Function DOI
Éva Bertalan, Masae Konno, Marı́a del Carmen Marı́n

и другие.

The Journal of Physical Chemistry B, Год журнала: 2024, Номер 128(30), С. 7407 - 7426

Опубликована: Июль 18, 2024

Microbial pump rhodopsins are highly versatile light-driven membrane proteins that couple protein conformational dynamics with ion translocation across the cell membranes. Understanding how microbial use specific amino acid residues at key functional sites to control selectivity and pumping direction is of general interest for transporters, could guide site-directed mutagenesis optogenetics applications. To enable direct comparisons between different sequences we implement, first time, a unique

Язык: Английский

Процитировано

2
Ionizable networks mediate pH-dependent allostery in SH2 signaling proteins DOI Creative Commons
Papa Kobina Van Dyck, Luke Piszkin,

Elijah Gorski

и другие.

bioRxiv (Cold Spring Harbor Laboratory), Год журнала: 2024, Номер unknown

Опубликована: Авг. 21, 2024

Introduction Transient intracellular pH dynamics 1 regulate mammalian proliferation 2,3 , migration 4 and differentiation 5 . However, for many pH-dependent cell processes, the molecular mediators are unknown 6 Prior work identified histidine residues as switches in pH-sensitive proteins, but how other ionizable contribute to protein allostery is understudied. Here, we develop an silico computational pipeline identify putative proteins their mechanisms. We first apply this SHP2, a known signaling with uncharacterized mechanism. show wild-type SHP2 phosphatase activity vitro cells, mutation of H116 E252 non-titratable alanine abolishes function. also that c-Src previously unrecognized kinase, network again activity. Constant simulations support conserved allosteric mechanism binding inhibitory SH2 domains functional catalytic c-Src. our across domain-containing evolutionarily pH-sensing networks. Our results reveal regulator providing insight into normal biology diseases where pHi dysregulated, such cancer.

Язык: Английский

Процитировано

0
Retinal Chromophore Environment in an Inward Light-Driven Proton Pump Studied by Solid-state NMR and Hydrogen-Bond Network Analysis DOI

Marie Pinto,

Maryam Saliminasab,

Andrew Harris

и другие.

Physical Chemistry Chemical Physics, Год журнала: 2024, Номер 26(36), С. 24090 - 24108

Опубликована: Янв. 1, 2024

The mechanism of inward proton transport in a microbial rhodopsin suggested by solid-state NMR spectroscopy and molecular dynamics simulations.

Язык: Английский

Процитировано

0