WWP2
From Proteopedia
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| - | <scene name='84/848928/Linker/3'>Text To Be Displayed</scene>[[Image:WWP2 F2Scene.png|300px|right|thumb| WWP2 Overall]] | + | <scene name='84/848928/Linker/8'>Text To Be Displayed</scene><scene name='84/848928/Linker/3'>Text To Be Displayed</scene>[[Image:WWP2 F2Scene.png|300px|right|thumb| WWP2 Overall]] |
==Introduction== | ==Introduction== | ||
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361-407 is 2,3 Linker | 361-407 is 2,3 Linker | ||
407-477 is WW3 and WW4 | 407-477 is WW3 and WW4 | ||
| - | 489-870 is HECT | + | 489-870 is <scene name='84/848928/Linker/8'>HECT</scene> |
</StructureSection> | </StructureSection> | ||
Revision as of 19:21, 15 June 2020
Contents |
Introduction
WWP2 is a family member of Homologous to the E6-AP Carboxyl Terminus (HECT) E3 Ligases which accept a ubiquitin molecule from an enzyme upstream in the ubiquitination pathway and transfer the ubiquitin to a 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 do not covalently bond to the ubiquitin ligand. ---
Structure
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This is a default text for your page WWP2. Click above on edit this page to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia [1] or to the article describing Jmol [2] to the rescue.
Function
Disease
Relevance
Structural highlights
References
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
Proteopedia Page Contributors and Editors (what is this?)
Tihitina Y Aytenfisu, Hannah Campbell, Sandra B. Gabelli, Michal Harel
