WWP2
From Proteopedia
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<StructureSection load='5TJ8' size='350' side='right' caption='WWP2 Ubiquitin Ligase Full-length Structure (PDB entry [[5TJ8]])' scene=''> | <StructureSection load='5TJ8' size='350' side='right' caption='WWP2 Ubiquitin Ligase Full-length Structure (PDB entry [[5TJ8]])' scene=''> | ||
| - | WWP2 is a <scene name='84/848928/Overall/2'>monomer</scene> consisting of a C2 domain, four WW domains (labeled WW1-WW4) and a HECT domain. | + | WWP2 is a <scene name='84/848928/Overall/2'>monomer</scene> consisting of a C2 domain, four WW domains (labeled WW1-WW4) and a HECT domain. This protein is autoinhibited by the 2,3-linker; upon phosphorylation WWP2 changes conformation into a more active form that can bind ubiquitin or other substrates. |
</StructureSection> | </StructureSection> | ||
Revision as of 13:18, 16 June 2020
Contents |
Introduction
WWP2 is a type of ubiquitin protein ligase. More specifically, it is a member of the Homologous to the E6-AP Carboxyl Terminus (HECT) E3 Ligases class which accept a ubiquitin molecule from an enzyme upstream in the ubiquitination pathway and transfer the ubiquitin to a Lysine residue in the target signaling molecule or transcription factor. The thioester bond formation between an active site Cystine on HECT E3 Ligases and ubiquitin differentiates this family of enzymes from the more abundant RING family of ubiquitin ligases which mediate ubiquitin transfer through non-covalent interactions. Within HECT E3 Ligases, WWP2 falls into the NEDD4 family. NEDD4 E3 Ligases consist of an N-terminal C2 Domain, between 2-4 WW domains, and a C-terminal HECT domain.
Structure
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Function
Disease
Relevance
Structural highlights
References
1. A Tunable Brake for HECT Ubiquitin Ligases.,Chen Z, Jiang H, Xu W, Li X, Dempsey DR, Zhang X, Devreotes P, Wolberger C, Amzel LM, Gabelli SB, Cole PA Mol Cell. 2017 May 4;66(3):345-357.e6. doi: 10.1016/j.molcel.2017.03.020. PMID:2847587
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Tihitina Y Aytenfisu, Hannah Campbell, Sandra B. Gabelli, Michal Harel
