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J Mol Biol. 2006 Oct 13;363(1):137-47. Epub 2006 Jul 31.

Structure of the SCAN domain from the tumor suppressor protein MZF1.

Author information

1
Department of Biochemistry, Medical College of Wisconsin, 8701 Watertown Plank Road Milwaukee, WI 53226, USA.

Erratum in

  • J Mol Biol. 2007 Feb 9;366(1):346.

Abstract

The SCAN domain mediates interactions between members of a subfamily of zinc-finger transcription factors and is found in more than 60 C2H2 zinc finger genes in the human genome, including the tumor suppressor gene myeloid zinc finger 1 (MZF1). Glutathione-S-transferase pull-down assays showed that the MZF1 SCAN domain self-associates, and a Kd value of 600 nM was measured by intrinsic tryptophan fluorescence polarization. The MZF1 structure determined by NMR spectroscopy revealed a domain-swapped dimer. Each monomer consists of five alpha helices in two subdomains connected by the alpha2-alpha3 loop. Residues from helix 3 of each monomer compose the core of the dimer interface, while the alpha1-alpha2 loop and helix 2 pack against helices 3 and 5 from the opposing monomer. Comprehensive sequence analysis is coupled with the first high-resolution structure of a SCAN dimer to provide an initial view of the recognition elements that govern dimerization for this large family of transcription factors.

PMID:
16950398
PMCID:
PMC1941711
DOI:
10.1016/j.jmb.2006.07.063
[Indexed for MEDLINE]
Free PMC Article

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