Crystal structure of the SCAN domain from human paternally expressed gene 3 proteinCrystal structure of the SCAN domain from human paternally expressed gene 3 protein

Structural highlights

4bhx is a 2 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:X-ray diffraction, Resolution 1.95Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PEG3_HUMAN Induces apoptosis in cooperation with SIAH1A. Acts as a mediator between p53/TP53 and BAX in a neuronal death pathway that is activated by DNA damage. Acts synergistically with TRAF2 and inhibits TNF induced apoptosis through activation of NF-kappa-B (By similarity). Possesses a tumor suppressing activity in glioma cells.[1]

Publication Abstract from PubMed

Human paternally expressed gene 3 protein (PEG3) is a large multi-domain entity with diverse biological functions, including acting as a transcription factor. PEG3 contains twelve Cys2-His2 type zinc finger domains, extended regions of predicted disorder and at the N-terminus a SCAN domain. PEG3 has been identified as partner of the E3 ubiquitin-protein ligase Siah1, an association we sought to investigate. An efficient bacterial recombinant expression system of the human PEG3-SCAN domain was prepared and crystals appeared spontaneously when the protein was being concentrated after purification. The structure was determined at 1.95 A resolution and reveals a polypeptide fold of five helices in an extended configuration. An extensive dimerization interface, using almost a quarter of the solvent accessible surface, and key salt bridge interactions explain the stability of the dimer. Comparison with other SCAN domains reveals a high degree of conservation involving residues that contribute to the dimer interface. The PEG3-SCAN domain appears to constitute an assembly block, enabling PEG3 homo- or heterodimerization to control gene expression in a combinatorial fashion.

Structure of the SCAN Domain of Human Paternally Expressed Gene 3 Protein.,Rimsa V, Eadsforth TC, Hunter WN PLoS One. 2013 Jul 23;8(7):e69538. doi: 10.1371/journal.pone.0069538. Print 2013. PMID:23936039[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Kohda T, Asai A, Kuroiwa Y, Kobayashi S, Aisaka K, Nagashima G, Yoshida MC, Kondo Y, Kagiyama N, Kirino T, Kaneko-Ishino T, Ishino F. Tumour suppressor activity of human imprinted gene PEG3 in a glioma cell line. Genes Cells. 2001 Mar;6(3):237-47. PMID:11260267
  2. Rimsa V, Eadsforth TC, Hunter WN. Structure of the SCAN Domain of Human Paternally Expressed Gene 3 Protein. PLoS One. 2013 Jul 23;8(7):e69538. doi: 10.1371/journal.pone.0069538. Print 2013. PMID:23936039 doi:10.1371/journal.pone.0069538

4bhx, resolution 1.95Å

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