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The zinc finger-associated SCAN box is a conserved oligomerization domain.

A number of Cys(2)His(2) zinc finger proteins contain a highly conserved amino-terminal motif termed the SCAN domain. This element is an 80-residue, leucine-rich region that contains three segments strongly predicted to be alpha-helices. In this report, we show that the SCAN motif functions as an oligomerization domain mediating self-association or association with other proteins bearing SCAN domains. These findings suggest that the SCAN domain plays an important role in the assembly and function of this newly defined subclass of transcriptional regulators.

Pubmed ID: 10567577


  • Williams AJ
  • Blacklow SC
  • Collins T


Molecular and cellular biology

Publication Data

December 6, 1999

Associated Grants

  • Agency: NHLBI NIH HHS, Id: HL61001
  • Agency: NHLBI NIH HHS, Id: R37HL35716

Mesh Terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • COS Cells
  • Conserved Sequence
  • DNA-Binding Proteins
  • Humans
  • Kruppel-Like Transcription Factors
  • Molecular Sequence Data
  • Protein Binding
  • Repressor Proteins
  • Sequence Homology, Amino Acid
  • Zinc Fingers