Structural Biology

Users are involved in a wide range of structural biology projects focused on the folds, functions, interactions and dynamics of enzymes, receptors and signaling domains.

Local groups accessing HWB•NMR led in the establishment of major structural biology initiatives including:

Our structural biology users are funded by the BBSRC, Cancer Research UK, EU, MRC, Wellcome Trust and other funding agencies.

Recent discoveries include:

discovery of the first structure of a PtdIns(4)P-specific PH domain and its membrane tubulation mechanism (Lenoir et al, 2009)

characterization of the solution structure of the human protein tyrosine phosphatase PTPN7 (Jeeves et al, 2008)

SALMON, a new and improved NMR screening method to screen for protein ligands (C Ludwig, J Med Chem, 2008)

first structure of the endocytic domain that recognizes NPFxD receptor internalization signal (RK Mahadev, Embo J, 2007)

NMR PRE-based method to solve structures of peripheral membrane proteins on lipid micelles (F Dancea, Biophys J, 2007)

first demonstration of performance advantages of the 900 MHz system for oligosaccharide NMR analysis (CD Blundell, Carbohyd Res, 2006)

 

 

HWB NMR logoPorta domain protein

POTRA domain protein

Three dimensional structures of proteins provide valuable information about their functions, as well as vital clues to how to block their actions during disease.