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.
Williams
A J
AJ
Department of Pathology, Brigham and Women's Hospital, Boston, Massachusetts 02115, USA.
Blacklow
S C
SC
Collins
T
T
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D019556:COS Cells; D017124:Conserved Sequence; D004268:DNA-Binding Proteins / Q000145:classification / Q000235:genetics* / Q000378:metabolism; D006801:Humans; D051741:Kruppel-Like Transcription Factors; D008969:Molecular Sequence Data; D011485:Protein Binding; D012097:Repressor Proteins / Q000145:classification / Q000235:genetics / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D016335:Zinc Fingers
D004268:DNA-Binding Proteins; D051741:Kruppel-Like Transcription Factors; D012097:Repressor Proteins; C108013:ZKSCAN8 protein, human; C096886:ZNF165 protein, human; C107307:ZNF263 protein, human; C095634:ZNF174 protein, human