WWP2
From Proteopedia
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==Structure== | ==Structure== | ||
| - | <StructureSection load='5TJ8' size='350' side='right' caption='WWP2 Ubiquitin Ligase Full-length Structure (PDB entry [[5TJ8]])' scene=1''> | ||
| - | Green link for <scene name='84/848928/Linker/1'>Scene F2</scene> | ||
| - | <scene name='84/848928/Linker/3'>Green link</scene><scene name='84/848928/Linker/4'>Text To Be Displayed</scene> for Scene F1 | ||
The structure of WWP2 consists of a C2 domain, four WW domains (labeled WW1-WW4) and a HECT domain. | The structure of WWP2 consists of a C2 domain, four WW domains (labeled WW1-WW4) and a HECT domain. | ||
| + | WWP2 Ubiquitin Ligase Full-length Structure (PDB entry [[5TJ8]]) | ||
| - | 17-142 is<scene name='84/848928/Linker/9'> C2 Domain</scene> | ||
| - | 302-361 is WW1 and WW2 | ||
| - | 361-407 is 2,3 Linker | ||
| - | 407-477 is WW3 and WW4 | ||
| - | 489-870 is <scene name='84/848928/Linker/8'>HECT</scene> | ||
| - | |||
| - | </StructureSection> | ||
Revision as of 20:30, 15 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
The structure of WWP2 consists of a C2 domain, four WW domains (labeled WW1-WW4) and a HECT domain. WWP2 Ubiquitin Ligase Full-length Structure (PDB entry 5TJ8)
Function
Disease
Relevance
Structural highlights
References
Proteopedia Page Contributors and Editors (what is this?)
Tihitina Y Aytenfisu, Hannah Campbell, Sandra B. Gabelli, Michal Harel
