| Citation | David Stuart is distinguished in protein crystallography for his development of methods for the solution of difficult problems and the achievement of results of biological importance. His major work has been the crystal structure dermination of Foot and Mouth Disease Virus (FMDV) in collaboration with F.Brown and virology colleagues. The X-ray crystallography presented formidable difficulties and the structure revealed new information on the organisation, antigenic properties and the host cell recognition properties of the virus. A peptide loop, that is known to be involved both in immune recognition and cell attachment, was found to be disordered in the native structure but after a minor chemical modification the loop was ordered to reveal the structure of the arginine-glycerine-aspartic acid (RGD) triplet that is involved in cell attachment. In a virus which escaped immune detection, the peptide loop was shown to be sensitive to changes remote in sequence leading to proposals for a confomational switch mechanism for escape from neutralising antibodies. This work has been complemented by structure solution of tumour necrosis factor, a cell adhesion molecule (CD2) and the structures of several different subtypes and serotypes of FMDV and a plant virus to build a substantial portfolio of structures that address problems of immune recognition of viruses, structural basis of protein/cell interactions and cell/cell adhesion. In earlier work David Stuart has made notable contributions with innovative methods to structural studies on pyruvate kinase, glycogen phosphroylase, a-lactalbumin and a modified insulin (work carried out in China). |