WWP2

From Proteopedia

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[[Image:WWP2 F2Scene.png|300px|right|thumb| WWP2 Overall]]
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==Introduction==
==Introduction==
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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=''>
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17-142 is C2 Domain
17-142 is C2 Domain

Revision as of 19:15, 15 June 2020

WWP2 Overall
WWP2 Overall

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

WWP2 Ubiquitin Ligase Full-length Structure (PDB entry 5TJ8)

Drag the structure with the mouse to rotate


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

  1. ↑ 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
  2. ↑ 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

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