Cullin

spinqualitylabelsall models Human cullin-1 (cyan) complex with ring box protein 1 (green) and Zn+2 ion (grey) (PDB code 1ldj) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Cullins are hydrophobic scaffold proteins for E3 ubiquitin ligases. They combine with ring box proteins (RBX) to form the CRL complex. 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. Cullin-2 is part of the ECS (Elongin-cullin-SOCS-box) complex. Cullin-3 is part of the BTB-Cul3 complex. Cullin-4A and 4B regulate various processes like DNA repair, chromatin remodeling and mitotic cell cycle. Cullin-5 inhibits cellular proliferation. Cullin-7 is a core component of a complex which mediates ubiquitination of target proteins. Human cullin-1 complex with ring box protein 1 and Zn+2 ions. 1st Zn coordination site. 2nd Zn coordination site. 3rd Zn coordination site.(PDB code 1ldj) 3D Structures of cullin Cullin 3D structures

3D Structures of cullin

Updated on 20-May-2019

{"openlevels":0}

• Cullin-1
  • 1ldj – hCul1 + RBX1 – human
    
  • Cullin 3D structures – hCul1 residues 411-766 (mutant) + RBX1
    
  • 5v89 – hCul1 WHB domain residues 702-776 + Dcn1-like protein
    
  • 3tdu – hCul1 WHB domain + Dcn1-like protein + NEDD8-conjugating enzyme Ubc12
    
  • 3tdz – hCul1 WHB domain + 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 + elongin-C
    
  • 5n4w – hCul2 + PVHL + elongin-B + elongon-C + RBX1 +
    
• Cullin-3
  • 5nlb – hCul3 N terminal + kelch-like protein
    
  • 6i2m – hCul3 (mutant) + kelch-repeat protein
    
  • 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

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