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Rob Smock
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 The E. coli DnaK peptide binding domain (left) and ATPase domain (right) with
ligands shown in red.
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I'm investigating the allosteric mechanism in Hsp70 proteins using a statistical analysis of the family’s evolutionary record. A network of interacting residues can be shown by extracting co-conserved position pairs from a multiple sequence alignment. Painting this network on the single domain crystal structures of our Hsp70 of interest, E. coli DnaK, reveals surface patches that may implicate an orientation for domain packing. Normal mode analysis and computational docking were combined with the statistical approach to generate domain docking models. These models provide the basis for designing cysteine mutations, which could allow the two domains to be bridged by disulfides or cross-linkers in the full-length protein and perhaps verify the model for domain orientation.
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