Document Detail


Solution structure of a zinc finger domain of yeast ADR1.
MedLine Citation:
PMID:  2114025     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The "zinc finger" is a 30-residue repeating motif that has been identified in a variety of eukaryotic transcription factors. Each domain is capable of binding a Zn2+ ion through invariant Cys and His residues. We have determined the three-dimensional structure of a synthetic peptide that corresponds to one of the two zinc finger domains in the yeast transcription factor ADR1, using two-dimensional nuclear magnetic resonance spectroscopy. The Zn2(+)-bound structure of the peptide consists of a loop containing the two Cys residues, a "fingertip," a 12- to 13-residue alpha-helix containing the two His residues, and a C-terminal tail. A majority of the interresidue contacts observed involve the seven conserved residues of the prototypic zinc finger (i.e., the four zinc ligands and the three hydrophobic residues), indicating that these residues are largely responsible for the three-dimensional structure of the domain and that all the zinc finger domains of the TFIIIA class will have similar structures. Potential DNA-binding residues are found throughout the structure, with the highest concentration of such residues on the external face of the alpha-helix.
Authors:
R E Klevit; J R Herriott; S J Horvath
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Proteins     Volume:  7     ISSN:  0887-3585     ISO Abbreviation:  Proteins     Publication Date:  1990  
Date Detail:
Created Date:  1990-08-08     Completed Date:  1990-08-08     Revised Date:  2008-10-23    
Medline Journal Info:
Nlm Unique ID:  8700181     Medline TA:  Proteins     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  215-26     Citation Subset:  IM    
Affiliation:
Department of Biochemistry, University of Washington, Seattle 98195.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Binding Sites
DNA-Binding Proteins*
Fungal Proteins*
Magnetic Resonance Spectroscopy
Metalloproteins*
Molecular Sequence Data
Protein Conformation
Saccharomyces cerevisiae / genetics*
Saccharomyces cerevisiae Proteins*
Transcription Factor TFIIIA
Transcription Factors*
Zinc / metabolism
Grant Support
ID/Acronym/Agency:
2 PO1 32681//PHS HHS
Chemical
Reg. No./Substance:
0/ADR1 protein, S cerevisiae; 0/DNA-Binding Proteins; 0/Fungal Proteins; 0/Metalloproteins; 0/Saccharomyces cerevisiae Proteins; 0/Transcription Factor TFIIIA; 0/Transcription Factors; 7440-66-6/Zinc

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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