WWP2: Difference between revisions

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The HECT domain is divided into two lobes (labeled N and C). The N-lobe serves as a binding site for the E2-ubiquitin complex and includes an exosite for non-covalent ubiquitin binding relevant to autoinhibition while the C-lobe contains an active site with a catalytic Cys residue to which the substrate ubiquitin molecule can covalently attach. The <scene name='84/848928/Hinge_zoomed/7'>hinge</scene> (magenta) connects the N and C lobes of the HECT domain and allows for flexible movement of the lobes as ubiquitin is transferred from the E2-ubiquitin complex docked on the N-lobe to the ubiquitin binding site in the C-lobe. A transthiolation reaction in this active site results in a thioester bond between the ubiquitin and a Cys residue. The HECT domain is in an inverse T shape when inactive (autoinhibited) and takes on an L shape when active. WW2 interaction with HECT is mediated by the six C terminal residues.
The HECT domain is divided into two lobes (labeled N and C). The N-lobe serves as a binding site for the E2-ubiquitin complex and includes an exosite for non-covalent ubiquitin binding relevant to autoinhibition while the C-lobe contains an active site with a catalytic Cys residue to which the substrate ubiquitin molecule can covalently attach. The <scene name='84/848928/Hinge_zoomed/7'>hinge</scene> (magenta) connects the N and C lobes of the HECT domain and allows for flexible movement of the lobes as ubiquitin is transferred from the E2-ubiquitin complex docked on the N-lobe to the ubiquitin binding site in the C-lobe. A transthiolation reaction in this active site results in a thioester bond between the ubiquitin and a Cys residue. The HECT domain is in an inverse T shape when inactive (autoinhibited) and takes on an L shape when active. WW2 interaction with HECT is mediated by the six C terminal residues.
<html5media height="360" width="360">https://vimeo.com/540291073</html5media>
<html5media height="360" width="640">https://vimeo.com/540291073</html5media>


The video above shows the protein WWP2, with emphasis on the hinge loop shown in magenta.
The video above shows the protein WWP2, with emphasis on the hinge loop shown in magenta.