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 studied structure shows both | The studied structure shows both <scene name='86/868189/Catalytic_site_polyubiquitine/1'>the catalytic site and polyubiquitin-C</scene>. | ||
== Biological role == | == Biological role == | ||
