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Why is this important?
We want to pinpoint the specific protease(s) which confer the invasive and metastatic potential to cells.
Metalloproteases represent the most densely populated class of proteolytic enzymes in humans and are thought to play a key role in the degradation of the extracellular matrix (ECM), enabling cancer cell invasion, migration, and metastasis.
Some pockets are naturally occurring while others are hidden, being revealed by conformational changes or induced by ligand binding.
Canonical binding sites are evolutionarily conserved and related proteins have structurally similar binding pockets. Cancer cells sometimes alter proteins by mutating or deleting amino acids in or around known binding sites.
We want to identify ligandable pockets on select metalloprotease family members and use this information to construct a roadmap which we can use to identify and characterize how drugs, ligands and chemical compounds interact across this protease family.