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| <StructureSection load='1ldj' size='340' side='right' caption='Human cullin-1 (grey) complex with ring box protein 1 (green) and Zn+2 ion (grey) (PDB code [[1ldj]])' scene=''> | | <StructureSection load='1ldj' size='340' side='right' caption='Human cullin-1 (grey) complex with ring box protein 1 (green) and Zn+2 ion (grey) (PDB code [[1ldj]])' scene=''> |
| '''Cullins''' are hydrophobic scaffold proteins for E3 ubiquitin ligases. They combine with ring box proteins (RBX) to form the CRL complex.<ref>PMID:15688063</ref> The CRL complex is essential in targeting proteins to ubiquitin-mediated destruction. Cullin-1 to 7 are part of the multi-subunit ubiquitin complex. Conjugation of cullin to NEDD8 modulates the activation of the CRL.<br /> | | '''Cullins''' are hydrophobic scaffold proteins for E3 ubiquitin ligases. They combine with ring box proteins (RBX) to form the CRL complex.<ref>PMID:15688063</ref> The CRL complex is essential in targeting proteins to ubiquitin-mediated destruction. Cullin-1 to 7 are part of the multi-subunit ubiquitin complex. Conjugation of cullin to NEDD8 modulates the activation of the CRL.<br /> |
| *'''Cullin-1''' is part of the SCF (Skp-cullin-F-box containing) complex which catalyzes the ubiquitination of proteins.<br /> | | *'''Cullin-1''' is part of the SCF (Skp-cullin-F-box containing) complex which catalyzes the ubiquitination of proteins.<ref>PMID:11961546</ref><br /> |
| *'''Cullin-2''' is part of the ECS (Elongin-cullin-SOCS-box) complex.<br /> | | *'''Cullin-2''' is part of the ECS (Elongin-cullin-SOCS-box) complex.<br /> |
| *'''Cullin-3''' is part of the BTB-Cul3 complex. <br /> | | *'''Cullin-3''' is part of the BTB-Cul3 complex.<ref>PMID:23349464</ref> <br /> |
| *'''Cullin-4A and 4B''' regulate various processes like DNA repair, chromatin remodeling and mitotic cell cycle.<br /> | | *'''Cullin-4A and 4B''' regulate various processes like DNA repair, chromatin remodeling and mitotic cell cycle.<ref>PMID:22118460</ref><br /> |
| *'''Cullin-5''' inhibits cellular proliferation.<br /> | | *'''Cullin-5''' inhibits cellular proliferation.<ref>PMID:18805092</ref><br /> |
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| </StructureSection> | | </StructureSection> |
Revision as of 11:56, 15 December 2015
| Cullins are hydrophobic scaffold proteins for E3 ubiquitin ligases. They combine with ring box proteins (RBX) to form the CRL complex.[1] The CRL complex is essential in targeting proteins to ubiquitin-mediated destruction. Cullin-1 to 7 are part of the multi-subunit ubiquitin complex. Conjugation of cullin to NEDD8 modulates the activation of the CRL.
- Cullin-1 is part of the SCF (Skp-cullin-F-box containing) complex which catalyzes the ubiquitination of proteins.[2]
- Cullin-2 is part of the ECS (Elongin-cullin-SOCS-box) complex.
- Cullin-3 is part of the BTB-Cul3 complex.[3]
- Cullin-4A and 4B regulate various processes like DNA repair, chromatin remodeling and mitotic cell cycle.[4]
- Cullin-5 inhibits cellular proliferation.[5]
- ↑ Petroski MD, Deshaies RJ. Function and regulation of cullin-RING ubiquitin ligases. Nat Rev Mol Cell Biol. 2005 Jan;6(1):9-20. PMID:15688063 doi:https://dx.doi.org/10.1038/nrm1547
- ↑ Zheng N, Schulman BA, Song L, Miller JJ, Jeffrey PD, Wang P, Chu C, Koepp DM, Elledge SJ, Pagano M, Conaway RC, Conaway JW, Harper JW, Pavletich NP. Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex. Nature. 2002 Apr 18;416(6882):703-9. PMID:11961546 doi:https://dx.doi.org/10.1038/416703a
- ↑ Canning P, Cooper CD, Krojer T, Murray JW, Pike AC, Chaikuad A, Keates T, Thangaratnarajah C, Hojzan V, Marsden BD, Gileadi O, Knapp S, von Delft F, Bullock AN. Structural basis for Cul3 assembly with the BTB-Kelch family of E3 ubiquitin ligases. J Biol Chem. 2013 Jan 24. PMID:23349464 doi:https://dx.doi.org/10.1074/jbc.M112.437996
- ↑ Fischer ES, Scrima A, Bohm K, Matsumoto S, Lingaraju GM, Faty M, Yasuda T, Cavadini S, Wakasugi M, Hanaoka F, Iwai S, Gut H, Sugasawa K, Thoma NH. The Molecular Basis of CRL4(DDB2/CSA) Ubiquitin Ligase Architecture, Targeting, and Activation. Cell. 2011 Nov 23;147(5):1024-39. PMID:22118460 doi:10.1016/j.cell.2011.10.035
- ↑ Duda DM, Borg LA, Scott DC, Hunt HW, Hammel M, Schulman BA. Structural insights into NEDD8 activation of cullin-RING ligases: conformational control of conjugation. Cell. 2008 Sep 19;134(6):995-1006. PMID:18805092 doi:https://dx.doi.org/10.1016/j.cell.2008.07.022
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3D Structures of cullin
Updated on 15-December-2015
{"openlevels":0}
- Cullin-1
- 1ldj – hCul1 + RBX1 – human
- 3rtr – hCul1 residues 411-766 (mutant) + RBX1
- 3tdu – hCul1 residues 702-776 + Dcn1-like protein + NEDD8-conjugating enzyme Ubc12
- 3tdz – hCul1 residues 702-776 + Dcn1-like protein + stapled Ubc12 peptide
- 1ldk – hCul1 + RBX1 + cyclin A/Cdk2-asociated protein + Skp2-like protein
- 1u6g – hCul1 + RBX1 + TIP120 protein
- 4f52 – hCul1 residues 411-690 (mutant) + RBX1 + glomulin
- 4p5o – hCul1 residues 411-776 + Dcn1-like protein + NEDD8-conjugating enzyme Ubc12 + RBX1 + NEDD8-conjugating enzyme Ubc12 + NEDD8
- Cullin-2
- 4wqo – hCul2 residues 20-122 + PVHL + transcription elongation factor B
- Cullin-3
- 4ap2, 4apf, 4hxi – hCul3 N terminal (mutant) + kelch-like protein
- 4eoz – hCul3 N terminal (mutant) + peckle-type POZ protein
- 2myl, 2mym – hCul3 residues 49-68 - NMR
- Cullin-4A
- 2hye – hCul4A + RBX1 + DNA damage-binding protein 1 + nonstructural protein
- 4a0k – hCul4A + RBX1 + DNA damage-binding protein 1 + DNA damage-binding protein 2 + DNA
- Cullin-4B
- 4a64 – hCul4B residues 188-539
- 2do7 – hCul4B winged helix-turn-helix - NMR
- 4a0c – hCul4B residues 192-913 + RBX1 + cullin-associated NEDD8-dissociated protein
- 4a0l – hCul4B + RBX1 + DNA damage-binding protein 1 + DNA damage-binding protein 2 + DNA
- Cullin-5
- 2wzk – hCul5 N terminal (mutant)
- 3dpl – hCul5 residues 401-780 (mutant) + RBX1
- 3dqv – hCul5 residues 401-780 (mutant) + RBX1 + NEDD8
- 4jgh – hCul5 N terminal (mutant) + SOCS-2 + transcription elongation factor B
- 4n9f – hCul5 N terminal + core-binding factor + virion infectivity factor + transcription elongation factor B
- Cullin-7
- 2jng – hCul7 residues 360-460 - NMR
- Cullin-A
- 3o2p, 3o6b – CulA residues 730-815 + defective in cullin neddylation protein - yeast
References
