Protein-peptide complex crystallization: a case study on the ERK2 mitogen-activated protein kinase.

ABSTRACT: Linear motifs normally bind with only medium binding affinity (Kd of ∼0.1-10 µM) to shallow protein-interaction surfaces on their binding partners. The crystallization of proteins in complex with linear motif-containing peptides is often challenging because the energy gained upon crystal packing between symmetry mates in the crystal may be on a par with the binding energy of the protein-peptide complex. Furthermore, for extracellular signal-regulated kinase 2 (ERK2) the protein-peptide docking surface is comprised of a small hydrophobic surface patch that is often engaged in the crystal packing of apo ERK2 crystals. Here, a rational surface-engineering approach is presented that involves mutating protein surface residues that are distant from the peptide-binding ERK2 docking groove to alan

SUBMITTER: Gogl G 

PROVIDER: S-EPMC3605046 | biostudies-literature | 2013 Mar

REPOSITORIES: biostudies-literature