Ubiquitin protein ligase
From Proteopedia
(Difference between revisions)
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**[[2h0d]] – mUPL RING domain + B lymphoma MO-MLV insertion region <br /> | **[[2h0d]] – mUPL RING domain + B lymphoma MO-MLV insertion region <br /> | ||
| - | *'''Ubiquitin protein ligase RNF or ring finger protein''' Domains: PUB 1-184; catalytic 853-1072; | + | *'''Ubiquitin protein ligase RNF or ring finger protein''' Domains: PUB 1-184; RING 216-290; catalytic 853-1072; |
**[[4ppe]], [[3ng2]] – hUPL 4 RING domain <br /> | **[[4ppe]], [[3ng2]] – hUPL 4 RING domain <br /> | ||
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**[[4orh]] – hUPL 8 residues 345-485 + E2 N <br /> | **[[4orh]] – hUPL 8 residues 345-485 + E2 N <br /> | ||
**[[4whv]] – hUPL 8 residues 345-485 + ubiquitin + E2 N <br /> | **[[4whv]] – hUPL 8 residues 345-485 + ubiquitin + E2 N <br /> | ||
| + | **[[5zc4]] – hUPL 13 RING domain <br /> | ||
**[[5d1k]], [[5d1l]], [[5d1m]] – hUPL 25 residues 126-258 + E2 D2 <br /> | **[[5d1k]], [[5d1l]], [[5d1m]] – hUPL 25 residues 126-258 + E2 D2 <br /> | ||
**[[4juy]], [[4oyj]], [[4p09]] – hUPL 31 PUB domain <br /> | **[[4juy]], [[4oyj]], [[4p09]] – hUPL 31 PUB domain <br /> | ||
| - | **[[4ljq]] – hUPL 31 catalytic domain <br /> | + | **[[4ljq]], [[6gzy]] – hUPL 31 catalytic domain <br /> |
| + | **[[6sc6]] – hUPL 31 catalytic domain + antibody<br /> | ||
| + | **[[6sc5]], [[6sc7]], [[6sc8]], [[6sc9]] – hUPL 31 catalytic domain + antibody + inhibitor<br /> | ||
**[[4ljo]] – hUPL 31 catalytic domain + ubiquitin<br /> | **[[4ljo]] – hUPL 31 catalytic domain + ubiquitin<br /> | ||
**[[5edv]] – hUPL 31 catalytic domain + ubiquitin + E2<br /> | **[[5edv]] – hUPL 31 catalytic domain + ubiquitin + E2<br /> | ||
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**[[5x0w]] – hUPL 31 residues 480-639 + Sharpin <br /> | **[[5x0w]] – hUPL 31 residues 480-639 + Sharpin <br /> | ||
**[[5y3t]] – hUPL 31 residues 474-630 + Sharpin + HOIL-7 <br /> | **[[5y3t]] – hUPL 31 residues 474-630 + Sharpin + HOIL-7 <br /> | ||
| + | **[[5zbu]] – hUPL 31 RING domain (mutant) + ubiquitin-C + E2 D2<br /> | ||
**[[4v3k]], [[4v3l]] – hUPL 38 residues 439-515 + polyubiquitin-C + E2 D2<br /> | **[[4v3k]], [[4v3l]] – hUPL 38 residues 439-515 + polyubiquitin-C + E2 D2<br /> | ||
**[[4kng]] – hUPL 43 PA domain + LGR5 + RSPO1<br /> | **[[4kng]] – hUPL 43 PA domain + LGR5 + RSPO1<br /> | ||
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**[[5d0k]], [[5d0m]], [[5ulh]], [[5ulk]] – hUPL 165 residues 255-348 + ubiquitin + E2 D2 <br /> | **[[5d0k]], [[5d0m]], [[5ulh]], [[5ulk]] – hUPL 165 residues 255-348 + ubiquitin + E2 D2 <br /> | ||
**[[3l11]], [[4gb0]] – hUPL 168 RING domain <br /> | **[[3l11]], [[4gb0]] – hUPL 168 RING domain <br /> | ||
| - | **[[5xis]] – hUPL 168 residues 110-188 + diubiquitin <br /> | + | **[[5xis]], [[5ydk]] – hUPL 168 residues 110-188 + diubiquitin <br /> |
| + | **[[5vey]] – hUPL 169 residues 653-708 + polyubiquitin + histone 2B - NMR<br /> | ||
| + | **[[5zi6]] – hUPL 194 residues 605-659<br /> | ||
**[[2rsf]] – mUPL 146 WWE domain + ATP<br /> | **[[2rsf]] – mUPL 146 WWE domain + ATP<br /> | ||
**[[4qpl]] – mUPL 146 RING+WWE domains + E2<br /> | **[[4qpl]] – mUPL 146 RING+WWE domains + E2<br /> | ||
Revision as of 08:18, 22 March 2020
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3D Structures of ubiquitin protein ligase
Updated on 22-March-2020
References
- ↑ Ardley HC, Robinson PA. E3 ubiquitin ligases. Essays Biochem. 2005;41:15-30. PMID:16250895 doi:http://dx.doi.org/10.1042/EB0410015
- ↑ Sakemi R, Yano H, Ogasawara S, Akiba J, Nakashima O, Fukahori S, Sata M, Kojiro M. X-linked inhibitor of apoptosis (XIAP) and XIAP-associated factor-1 expressions and their relationship to apoptosis in human hepatocellular carcinoma and non-cancerous liver tissues. Oncol Rep. 2007 Jul;18(1):65-70. PMID:17549347
- ↑ Aguilar C, Lenoir C, Lambert N, Begue B, Brousse N, Canioni D, Berrebi D, Roy M, Gerart S, Chapel H, Schwerd T, Siproudhis L, Schappi M, Al-Ahmari A, Mori M, Yamaide A, Galicier L, Neven B, Routes J, Uhlig HH, Koletzko S, Patel S, Kanegane H, Picard C, Fischer A, Bensussan NC, Ruemmele F, Hugot JP, Latour S. Characterization of Crohn disease in X-linked inhibitor of apoptosis-deficient male patients and female symptomatic carriers. J Allergy Clin Immunol. 2014 Nov;134(5):1131-41.e9. doi:, 10.1016/j.jaci.2014.04.031. Epub 2014 Jun 15. PMID:24942515 doi:http://dx.doi.org/10.1016/j.jaci.2014.04.031
- ↑ Ardley HC, Robinson PA. The role of ubiquitin-protein ligases in neurodegenerative disease. Neurodegener Dis. 2004;1(2-3):71-87. PMID:16908979 doi:http://dx.doi.org/10.1159/000080048
- ↑ Xu G, Jiang X, Jaffrey SR. A mental retardation-linked nonsense mutation in cereblon is rescued by proteasome inhibition. J Biol Chem. 2013 Oct 11;288(41):29573-85. doi: 10.1074/jbc.M113.472092. Epub, 2013 Aug 27. PMID:23983124 doi:http://dx.doi.org/10.1074/jbc.M113.472092
- ↑ Lu G, Middleton RE, Sun H, Naniong M, Ott CJ, Mitsiades CS, Wong KK, Bradner JE, Kaelin WG Jr. The myeloma drug lenalidomide promotes the cereblon-dependent destruction of Ikaros proteins. Science. 2014 Jan 17;343(6168):305-9. doi: 10.1126/science.1244917. Epub 2013 Nov, 29. PMID:24292623 doi:http://dx.doi.org/10.1126/science.1244917
- ↑ Stieglitz B, Rana RR, Koliopoulos MG, Morris-Davies AC, Schaeffer V, Christodoulou E, Howell S, Brown NR, Dikic I, Rittinger K. Structural basis for ligase-specific conjugation of linear ubiquitin chains by HOIP. Nature. 2013 Oct 20. doi: 10.1038/nature12638. PMID:24141947 doi:http://dx.doi.org/10.1038/nature12638
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