The receptor is active in clearing a number of proteases bound to a 2 -macroglobulinfrom circulation by endocytosis. This protein presumably regulates the internalization of the a 2 -macroglobulin receptor. We have determined the structure of the first module. Long term plans are to study photo induced protein folding directly by NMR at the highest sensitivity at 18.8 Tesla. Several of the research projects of the institute are concerned with proteins that play important roles in these key biological processes.
Signal transduction is important for numerous processes in regulating cellular functions.
The signalling can be stimulated in several ways and the paths of signal transduction involve many different proteins. At present we are engaging in studies of a number of proteins from the signal transduction pathways of several cellular processes in plants and in animal cells. Although the structure of tetranectin has been determined by X-ray crystallography it has not been possible to crystallize the calcium free carbohydrate recognition domain which is the form that binds to kringle 4 of plasminogen. It is also planned to determine the structure of the complex between plasminogen kringle 4 and the carbohydrate recognition domain of tetranectin. All the proteins have been expressed and initial NMR studies have documented the feasibility of these projects.