Δημοσιεύσεις

Project Acronym: Kras
Title: Uncovering the full free energy landscape of KRAS for computer-aided drug design
Affiliation: biomedical research foundation - academy of athens
Pi: Zoe Cournia
Research Field: biochemistry, bioinformatics and life sciences

Allostery in membrane proteins
by Zoe Cournia, AlexiosChatzigoulas
Abstract:
Membrane proteins are an integral part of signal transduction. To signal, membrane proteins must interact with a variety of lipid species, effectors, and other proteins in the biological membrane leading to an immense number of possible interactions. Despite this inherent complexity, accurate control of signaling must take place. By allowing proteins to adopt a multiplicity of conformations in a process known as allostery, nature is able to transmit a signal from one protein site to another distal, functional site, allowing for modulation of protein properties and regulation of activity. In recent years, an increasing number of reports have pointed to common mechanisms governing the allosteric modulation of membrane proteins, including conformational selection, oligomerization, and the modulation of allosteric sites. In this report, we summarize recent advances in membrane protein allostery.
Reference:
Allostery in membrane proteins (Zoe Cournia, AlexiosChatzigoulas), In Current Opinion in Structural Biology, volume 62, 2020.
Bibtex Entry:
@article{doi:10.1016-j.sbi.2020.03.006,
 author = {Zoe Cournia, AlexiosChatzigoulas},
 doi = {10.1016/j.sbi.2020.03.006},
 url = {https://doi.org/10.1016/j.sbi.2020.03.006},
 year = {2020},
 bibyear = {2020},
 journal = {Current Opinion in Structural Biology},
 volume = {62},
 pages = {197-204},
 title = {Allostery in membrane proteins},
 abstract = {Membrane proteins are an integral part of signal transduction. To signal, membrane proteins must interact with a variety of lipid species, effectors, and other proteins in the biological membrane leading to an immense number of possible interactions. Despite this inherent complexity, accurate control of signaling must take place. By allowing proteins to adopt a multiplicity of conformations in a process known as allostery, nature is able to transmit a signal from one protein site to another distal, functional site, allowing for modulation of protein properties and regulation of activity. In recent years, an increasing number of reports have pointed to common mechanisms governing the allosteric modulation of membrane proteins, including conformational selection, oligomerization, and the modulation of allosteric sites. In this report, we summarize recent advances in membrane protein allostery.},
}