User:Jquick2019/Ubiquitin-conjugating enzyme
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Edit summary[edit]
Copied over the Relationships section from the article Ubiquitin-conjugating enzyme then added some information inside of the second paragraph. I then created the structure heading which will be filled out more in the future.
Relationships[edit]
A ubiquitin-activating enzyme, or E1, first activates the ubiquitin by covalently attaching the molecule to its active site cysteine residue. The activated ubiquitin is then transferred to an E2 cysteine. Once conjugated to ubiquitin, the E2 molecule binds one of several ubiquitin ligases or E3s via a structurally conserved binding region. The E3 molecule is responsible for binding the target protein substrate and transferring the ubiquitin from the E2 cysteine to a lysine residue on the target protein.[1]
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Schematic diagram of the ubiquitylation system.
A particular cell usually contains only a few types of E1 molecule, a greater diversity of E2s, and a very large variety of E3s. In humans, there are about 30 E2s which can bind with one of the 600+ E3s.[2] The E3 molecules responsible for substrate identification and binding are thus the mechanisms of substrate specificity in proteasomal degradation. Each type of E2 can associate with many E3s.[3]
E2s can also be used to study protein folding mechanisms. Since the ubiquitylation system is shared across all organisms, studies can use modified E2 proteins in order to understand the overall system for how all organisms process proteins.[4] There are also some proteins which can act as both and E2 and an E3 containing domains which cover both E2 and E3 functionality.[5]
References[edit]
- ^ Nandi D, Tahiliani P, Kumar A, Chandu D (2006). "The ubiquitin-proteasome system" (PDF). Journal of Biosciences. 31 (1): 137–55. doi:10.1007/BF02705243. PMID 16595883. S2CID 21603835.
- ^ Burge, Rebecca J.; Damianou, Andreas; Wilkinson, Anthony J.; Rodenko, Boris; Mottram, Jeremy C. (2020-10-27). Clayton, Christine (ed.). "Leishmania differentiation requires ubiquitin conjugation mediated by a UBC2-UEV1 E2 complex". PLOS Pathogens. 16 (10): e1008784. doi:10.1371/journal.ppat.1008784. ISSN 1553-7374. PMC 7647121. PMID 33108402.
{{cite journal}}: CS1 maint: PMC format (link) CS1 maint: unflagged free DOI (link) - ^ Risseeuw EP, Daskalchuk TE, Banks TW, Liu E, Cotelesage J, Hellmann H, Estelle M, Somers DE, Crosby WL (2003). "Protein interaction analysis of SCF ubiquitin E3 ligase subunits from Arabidopsis". The Plant Journal. 34 (6): 753–67. doi:10.1046/j.1365-313X.2003.01768.x. PMID 12795696.
- ^ Henneberg, Lukas T.; Schulman, Brenda A. (2021-07-15). "Decoding the messaging of the ubiquitin system using chemical and protein probes". Cell Chemical Biology. 28 (7): 889–902. doi:10.1016/j.chembiol.2021.03.009. PMC 7611516. PMID 33831368.
{{cite journal}}: CS1 maint: PMC format (link) - ^ Chang, Shu-Chun; Zhang, Bo-Xiang; Ding, Jeak Ling (March 2022). "E2-E3 ubiquitin enzyme pairing - partnership in provoking or mitigating cancers". Biochimica et Biophysica Acta (BBA) - Reviews on Cancer. 1877 (2): 188679. doi:10.1016/j.bbcan.2022.188679.