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Heinemann Lab

Macromolecular Structure and Interaction


The Macromolecular Structure and Interaction Laboratory combines macromolecular crystallography with biochemical and biophysical approaches to elucidate the molecular basis of biological processes at atomic detail.

One major area of research is concerned with the regulation of gene expression at the transcriptional as well as translational level. We study promoter and enhancer recognition by transcription factors to understand their function in transcription initiation as well as RNA-binding proteins that ensure mRNA homeostasis by regulating mRNA maturation, transport, translation and degradation.

In a second major area of research, we address problems of intracellular protein transport and sorting. Recently, we have determined crystal structures of the abundant human AAA ATPase p97 bound to the adapter protein ASPL and revealed a novel mode of AAA ATPase regulation by UBX-domain proteins. Structure analyses of the transport protein particle (TRAPP) contributed to understanding the function of this complex in tethering transport vesicles at the cis-Golgi membrane.



Many biological processes can be studied at the atomic level where macromolecular structures and interactions may be analyzed in exquisite detail. In our laboratory, crystallographic analysis is combined with biochemical and biophysical experiments to explain biological functions and observe specific ligand binding to proteins. We are primarily interested in proteins interacting with nucleic acids, involved in vesicle transport, or linked to disease states.