Computational simulation of ligand docking to L-type pyruvate kinase subunit
Computational docking revealed binding sites of L-type pyruvate kinase N-domain in domains A and C of the protein. Peptide RRASVA and its phosphor-analogue were used to model the regulatory N-domain. Phosphorylation shifted the peptide binding from domain A to domain C. Shift of N-domain interaction site may explain switching on L-PK cooperativity by phosphorylation.
l-type pyruvate kinase n-terminal domain docking in protein regulatory phosphorylation putative n-terminal docking sites substrate affinity regulation switching in cooperativity