DPG Phi
Verhandlungen
Verhandlungen
DPG

Dresden 2017 – scientific programme

Parts | Days | Selection | Search | Updates | Downloads | Help

DY: Fachverband Dynamik und Statistische Physik

DY 3: Computational Biophysics (joint BP/DY)

DY 3.12: Talk

Monday, March 20, 2017, 12:45–13:00, ZEU 250

Mechanism of rhomboid intramembrane proteolysis — •Ana Nicoleta Bondar — Department of Physics, Freie Universität Berlin, Arnimallee 14, D-14195 Berlin, Germany

Intramembrane proteases are membrane-embedded proteins whose substrates are transmembrane protein segments. Reaction mechanisms of intramembrane proteases are important to understand, because these proteins are implicated in essential processes such as cell signalling. A fundamental open question is how specific lipid molecules participate in the reaction coordinate of intramembrane protease. We address this question with extensive all-atom molecular dynamics simulations of the intramembrane rhomboid protease from Escherichia coli, GlpG. The computations indicate coupling between lipid binding at the substrate docking-site region and the composition of the lipid membrane, highlighting the importance of lipid interactions for the reaction coordinate of the protease.

Work supported in part by the Excellence Initiative of the German Federal and State Governments provided via the Freie Universität Berlin, and and allocation of computing time from the North-German Supercomputing Center, HLRN (bec00076).

References

1. A.-N. Bondar. Biophysical mechanism of rhomboid proteolysis: setting a foundation for therapeutics. Seminars in Cell and Developmental Biology 10.1016/j.semcdb.2016.09.006, Accepted (2016).

2. A.-N. Bondar, C. del Val, and S. H. White. Rhomboid protease dynamics and lipid interactions. Structure 17: 395-405 (2009).

100% | Mobile Layout | Deutsche Version | Contact/Imprint/Privacy
DPG-Physik > DPG-Verhandlungen > 2017 > Dresden