Specificity of a protein-protein interface: local dynamics direct substrate recognition of effector caspases.

ABSTRACT: Proteases are prototypes of multispecific protein-protein interfaces. Proteases recognize and cleave protein and peptide substrates at a well-defined position in a substrate binding groove and a plethora of experimental techniques provide insights into their substrate recognition. We investigate the caspase family of cysteine proteases playing a key role in programmed cell death and inflammation, turning caspases into interesting drug targets. Specific ligand binding to one particular caspase is difficult to achieve, as substrate specificities of caspase isoforms are highly similar. In an effort to rationalize substrate specificity of two closely related caspases, we investigate the substrate promiscuity of the effector Caspases 3 and 7 by data mining (cleavage entropy) and by molecular dy

SUBMITTER: Fuchs JE 

PROVIDER: S-EPMC4282588 | biostudies-literature | 2014 Apr

REPOSITORIES: biostudies-literature