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J Biol Chem, Vol. 273, Issue 33, 20867-20876, August 14, 1998
From the The C-terminal binding protein (CtBP) has
previously been shown to bind to a highly conserved six-amino acid
motif very close to the C terminus of adenovirus early region 1A (Ad
E1A) proteins. We have developed an enzyme-linked immunosorbent assay
that has facilitated the screening of synthetic peptides identical or
similar to the binding site on Ad E1A for their ability to bind CtBP
and thus inhibit its interaction with Ad12 E1A. It has been shown that
amino acids both C-terminal and N-terminal to the original proposed
binding site contribute to the interaction of peptides with CtBP.
Single amino acid substitutions across the binding site appreciably
alter the Kd of the peptide for CtBP, indicative of
a marked reduction in the affinity of the peptide for CtBP. The
solution structures of synthetic peptides equivalent to the C termini
of both Ad5 and Ad12 E1A and two substituted forms of these have been
determined by proton NMR spectroscopy. Both the Ad12 and Ad5 peptides
dissolved in trifluoroethanol/water mixtures were found to adopt
regular secondary structural conformations seen as a series of
Structural Determinants Present in the C-terminal Binding
Protein Binding Site of Adenovirus Early Region 1A Proteins
,,,, and
Cancer Research Campaign Institute for
Cancer Studies, University of Birmingham, Edgbaston,
Birmingham B15 2TA, United Kingdom and the ¶ Institute of
Molecular Virology, St. Louis University Medical Center, St. Louis,
Missouri 63110
-turns. An Ad12 peptide bearing a substitution that resulted in only
very weak binding to CtBP (Ad12 L258G) was found to be random coil in
solution. However, a second mutant (Ad12 V256K), which bound to CtBP
rather more strongly (although not as well as the wild type), adopted a
conformation similar to that of the wild type. We conclude that
secondary structure (-turns) and an appropriate series of amino acid
side chains are necessary for recognition by CtBP.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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