Repository logo

Infoscience

  • English
  • French
Log In
Logo EPFL, École polytechnique fédérale de Lausanne

Infoscience

  • English
  • French
Log In
  1. Home
  2. Academic and Research Output
  3. Journal articles
  4. Effect of N-Terminal Myristoylation on the Active Conformation of Gα
 
research article

Effect of N-Terminal Myristoylation on the Active Conformation of Gα

Van Keulen, Siri C.  
•
Rothlisberger, Ursula  
2017
Biochemistry

G proteins are part of the G-protein-coupled receptor (GPCR) signal transduction cascade in which they transfer a signal from the membrane-embedded GPCR to other proteins in the cell. In the case of the inhibitory G-protein heterotrimer, permanent N-terminal myristoylation can transiently localize the G alpha(i) subunit at the membrane as well as crucially influence G alpha(i)'s function in the GTP-bound conformation. The attachment of lipids to proteins is known to be essential for membrane trafficking; however, our results suggest that lipidation is also important for protein-protein interactions during signal transduction. Here we investigate the effect of myristoylation on the structure and dynamics of soluble G alpha(i) and its possible implication for signal transduction. A 2 mu s classical molecular dynamics simulation of a myristoylated G alpha(i1)-GTP complex suggests that the myristoyl-induced conformational changes of the switch II and alpha helical domains create new possibilities for protein-protein interactions and emphasize the importance of permanent lipid attachment for the conformation proteins. and functional tunability of signaling proteins.

  • Files
  • Details
  • Metrics
Loading...
Thumbnail Image
Name

FullText.pdf

Type

Publisher's Version

Version

http://purl.org/coar/version/c_970fb48d4fbd8a85

Access type

openaccess

Size

2 MB

Format

Adobe PDF

Checksum (MD5)

3b354601e9364806967a34dfaf9135af

Logo EPFL, École polytechnique fédérale de Lausanne
  • Contact
  • infoscience@epfl.ch

  • Follow us on Facebook
  • Follow us on Instagram
  • Follow us on LinkedIn
  • Follow us on X
  • Follow us on Youtube
AccessibilityLegal noticePrivacy policyCookie settingsEnd User AgreementGet helpFeedback

Infoscience is a service managed and provided by the Library and IT Services of EPFL. © EPFL, tous droits réservés