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Structure of the SCAN domain from the tumor suppressor protein MZF1. J Mol Biol 2006 Oct 13;363(1):137-47

Date

09/05/2006

Pubmed ID

16950398

Pubmed Central ID

PMC1941711

DOI

10.1016/j.jmb.2006.07.063

Scopus ID

2-s2.0-33748804696   13 Citations

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.

Author List

Peterson FC, Hayes PL, Waltner JK, Heisner AK, Jensen DR, Sander TL, Volkman BF

Authors

Francis C. Peterson PhD Professor in the Biochemistry department at Medical College of Wisconsin
Brian F. Volkman PhD Professor in the Biochemistry department at Medical College of Wisconsin




MESH terms used to index this publication - Major topics in bold

Amino Acid Sequence
DNA-Binding Proteins
Dimerization
Humans
Intracellular Signaling Peptides and Proteins
Kruppel-Like Transcription Factors
Models, Chemical
Models, Molecular
Molecular Sequence Data
Protein Structure, Tertiary
Transcription Factors
Zinc Fingers
jenkins-FCD Prod-444 eb4ebd1a08581aba961d3befd3b851a3c3ec6b46