Intrinsic allosteric inhibition of signaling proteins by targeting rare interaction states detected by high-pressure NMR spectroscopy

Angew Chem Int Ed Engl. 2013 Dec 23;52(52):14242-6. doi: 10.1002/anie.201305741. Epub 2013 Nov 11.

Authors

Hans Robert Kalbitzer¹, Ina C Rosnizeck, Claudia E Munte, Sunilkumar Puthenpurackal Narayanan, Veronika Kropf, Michael Spoerner

Affiliation

¹ Institute of Biophysics and Physical Biochemistry, Centre of Magnetic Resonance in Chemistry and Biomedicine (CMRCB), University of Regensburg, Universitätsstrasse 31, 93047 Regensburg (Germany). Hans-Robert.Kalbitzer@Biologie.Uni-Regensburg.de.

PMID: 24218090
DOI: 10.1002/anie.201305741

No abstract available

Keywords: Ras protein; allosteric inhibition; conformational states; drug design; high-pressure NMR spectroscopy.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Allosteric Regulation
Drug Design
Magnetic Resonance Spectroscopy / methods*
Proteins / chemistry*
Signal Transduction

Substances

Proteins