Sandbox Reserved 1656: Difference between revisions
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Residues present in the catalytic site of DUBs are often in a '''non-functional orientation''' when the substrate is absent. Thus, when the substrate binds to the catalytic site of the enzyme, the site undergoes rearrangement and takes on a functional conformation. <ref>PMID:16537382</ref> The substrate opens and closes to allow the entry of the protein to be deubiquitinased. | Residues present in the catalytic site of DUBs are often in a '''non-functional orientation''' when the substrate is absent. Thus, when the substrate binds to the catalytic site of the enzyme, the site undergoes rearrangement and takes on a functional conformation. <ref>PMID:16537382</ref> The substrate opens and closes to allow the entry of the protein to be deubiquitinased. | ||
The enzyme take this configuration thanks to <scene name='86/868189/H_bonds_around_ser177/1'>many hydrogen bonds around Ser177.</scene> | The enzyme take this configuration thanks to <scene name='86/868189/H_bonds_around_ser177/1'>many hydrogen bonds around Ser177.</scene> This is why Phosphorylation is so important to the function of the enzyme. The phosphate group forms many links between substrate ubiquitin and a segment of the OTU domain. This is rare among the known structures of deubiquitinases. Phosphorylation-driven conformational change ressembles the one of kinases. | ||
== Biological role == | == Biological role == | ||
