In addition, our group has recently discovered an allosteric mechanism through which binding of ligand at a remote allosteric site orders the active site in Ras, suggesting a new mechanism for the intrinsic hydrolysis reaction. The active site is modulated by protein binding partners in both its regulation and in interaction with effector proteins which propagate signaling. Ras and its family members normally have a disordered active site, which explains the intrinsically slow rate of GTP hydrolysis measured for these enzymes in solution. The protein-protein interactions mediating signal transduction pathways in which these GTPases are involved result in diverse and highly specific biological outcomes, including the control of cell proliferation, cell motility, transport of proteins across the nuclear membrane and many others. The biological system studied in this lab involves a group of closely related members of the Ras superfamily of GTPases. We are also interested in how small ligands are able to mediate or interfere with these interactions. We are particularly interested in the protein-protein interactions that allow these assemblies to form in a specific manner. It is clear that macromolecular interactions are central to the proper functioning, regulation and specificity of any cellular process, for example, signaling, transport, and replication. Research in the Mattos Lab focuses on understanding the rules that govern the recognition, assembly and function of macromolecular complexes. GTPases of the Ras Family Protein Interactions Protein X-ray Crystallography Solvent Mapping of Protein Surfaces Structure Based Ligand Discovery
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