After many years work our structural studies on the isolated TrkA domain that binds NGF has come to fruition with a new paper in J. Med. Chem. (See below). This study describes the use of an NMR construct of the second extracellular domain of the TrkA receptor to probe small ligand binding at the NGF binding site. This will be the basis of the development of further ligand scaffolds designed to agonise or antagonise the function of this receptor. We would be interested to hear from other groups working with this system who might wish to collaborate on future studies.

 

(Shoemark DK, Williams C, Fahey MS, Watson JJ, Tyler SJ, Scoltock SJ, Ellis RZ, Wickenden E, Burton AJ, Hemmings JL, Bailey CD, Dawbarn D, Jane DE, Willis CL, Sessions RB, Allen SJ and Crump MP* (2015) Design and Nuclear Magnetic Resonance (NMR) Structure Determination of the Second Extracellular Immunoglobulin Tyrosine Kinase A (TrkAIg2) Domain Construct for Binding Site Elucidation in Drug Discovery. J. Med. Chem. 58, 767-777. http://pubs.acs.org/doi/abs/10.1021/jm501307e)