2FI2

Solution structure of the SCAN homodimer from MZF-1/ZNF42

2FI2 の概要

• エントリーDOI: 10.2210/pdb2fi2/pdb
• NMR情報: BMRB: 6957
• 分子名称: Zinc finger protein 42 (1 entity in total)
• 機能のキーワード: scan domain, znf-42, mzf-1, homodimer, transcription factor, structural genomics, psi, protein structure initiative, center for eukaryotic structural genomics, cesg, transcription
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus: P28698
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 21035.78

構造登録者

Volkman, B.F.,Peterson, F.C.,Sander, T.L.,Waltner, J.K.,Center for Eukaryotic Structural Genomics (CESG) (登録日: 2005-12-27, 公開日: 2006-01-17, 最終更新日: 2024-05-29)

主引用文献

Peterson, F.C.,Hayes, P.L.,Waltner, J.K.,Heisner, A.K.,Jensen, D.R.,Sander, T.L.,Volkman, B.F.
Structure of the SCAN domain from the tumor suppressor protein MZF1.
J.Mol.Biol., 363:137-147, 2006

PubMed 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.

PubMed: 16950398
DOI: 10.1016/j.jmb.2006.07.063

実験手法

SOLUTION NMR