Entry Date:
December 2, 2011

Keating Lab

Principal Investigator Amy Keating


The Keating Lab uss computational and experimental methods to study protein structure, function and interactions. The "bottom up" approach targets structurally conserved interaction domains and motifs, including coiled coils and Bcl-2 family proteins. Simple structures offer the possibility of obtaining a detailed and predictive understanding of how sequence and structure encode interaction specificity.

Protein-protein interactions play critical roles inside and outside the cell, maintaining structure, enabling motility, regulating signal transduction and assembling molecular machines. An outstanding goal in biology is to understand how protein interactions are determined by sequence and structure. Work in the Keating laboratory is focused on how interaction specificity allows some proteins to select one or a few interaction partners out of a large number of alternatives. This is especially important for paralogous gene families and for other protein interactions mediated by structurally conserved motifs.

Studies in the lab are focused on alpha-helical coiled coils and Bcl-2 family proteins because of their biological and medical importance, and because questions of specificity can be addressed most powerfully in model systems that are well characterized. We combine computational and experimental approaches to understand, predict and design protein interaction specificity. We also develop new computational and experimental methods to address problems in this area.