8h3q

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Cryo-EM Structure of the CAND1-Cul3-Rbx1 complexCryo-EM Structure of the CAND1-Cul3-Rbx1 complex

Structural highlights

8h3q is a 3 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Electron Microscopy, Resolution 3.76Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CAND1_HUMAN Enhances transcription from various types of promoters (By similarity). Regulatory protein that interferes with the assembly of the SCF (SKP1-CUL1-F-box protein) ubiquitin ligase complex and thereby down-regulates ubiquitination of target proteins. Prevents neddylation of CUL1 by physically blocking access to the neddylation site. Disrupts interactions between CUL1 and SKP1 and between CUL1 and F-box proteins.[1] [2] [3]

See Also

References

  1. Zheng J, Yang X, Harrell JM, Ryzhikov S, Shim EH, Lykke-Andersen K, Wei N, Sun H, Kobayashi R, Zhang H. CAND1 binds to unneddylated CUL1 and regulates the formation of SCF ubiquitin E3 ligase complex. Mol Cell. 2002 Dec;10(6):1519-26. PMID:12504026
  2. Liu J, Furukawa M, Matsumoto T, Xiong Y. NEDD8 modification of CUL1 dissociates p120(CAND1), an inhibitor of CUL1-SKP1 binding and SCF ligases. Mol Cell. 2002 Dec;10(6):1511-8. PMID:12504025
  3. Min KW, Hwang JW, Lee JS, Park Y, Tamura TA, Yoon JB. TIP120A associates with cullins and modulates ubiquitin ligase activity. J Biol Chem. 2003 May 2;278(18):15905-10. Epub 2003 Feb 27. PMID:12609982 doi:10.1074/jbc.M213070200

8h3q, resolution 3.76Å

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