4BHX

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

Summary for 4BHX

• Entry DOI: 10.2210/pdb4bhx/pdb
• Descriptor: PATERNALLY-EXPRESSED GENE 3 PROTEIN, DI(HYDROXYETHYL)ETHER, TRIETHYLENE GLYCOL, ... (5 entities in total)
• Functional Keywords: dna binding protein, peg3
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Nucleus : Q9GZU2
• Total number of polymer chains: 2
• Total formula weight: 24931.11

Authors

Rimsa, V.,Eadsforth, T.C.,Hunter, W.N. (deposition date: 2013-04-09, release date: 2013-04-17, Last modification date: 2023-12-20)

Primary citation

Rimsa, V.,Eadsforth, T.C.,Hunter, W.N.
Structure of the Scan Domain of Human Paternally Expressed Gene 3 Protein.
Plos One, 8:69538-, 2013

PubMed Abstract: 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 Å 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.

PubMed: 23936039
DOI: 10.1371/JOURNAL.PONE.0069538

Experimental method

X-RAY DIFFRACTION (1.95 Å)