The Zinc Finger-Associated SCAN Box Is a Conserved Oligomerization Domain | Zendy

Amy J. Williams | Zendy; Stephen C. Blacklow | Zendy; Tucker Collins | Zendy

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The Zinc Finger-Associated SCAN Box Is a Conserved Oligomerization Domain

Author(s) -

Amy J. Williams,

Stephen C. Blacklow,

Tucker Collins

Publication year - 1999

Publication title -

molecular and cellular biology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.14

H-Index - 327

eISSN - 1067-8824

pISSN - 0270-7306

DOI - 10.1128/mcb.19.12.8526

Subject(s) - zinc finger , biology , lim domain , ring finger domain , genetics , computational biology , motif (music) , structural motif , conserved sequence , protein domain , sequence motif , peptide sequence , microbiology and biotechnology , biochemistry , transcription factor , dna , gene , physics , acoustics

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.

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