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Science 21 April 1995:
Vol. 268. no. 5209, pp. 436 - 439
DOI: 10.1126/science.7716550
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Articles

Science, Vol 268, Issue 5209, 436-439
Copyright © 1995 by American Association for the Advancement of Science

articles

Measurement of interhelical electrostatic interactions in the GCN4 leucine zipper

KJ Lumb and PS Kim

Howard Hughes Medical Institute, Whitehead Institute for Biomedical Research, Department of Biology, Massachusetts Institute of Technology, Cambridge 02142, USA.

The dimerization specificity of the bZIP transcription factors resides in the leucine zipper region. It is commonly assumed that electrostatic interactions between oppositely charged amino acid residues on different helices of the leucine zipper contribute favorably to dimerization specificity. Crystal structures of the GCN4 leucine zipper contain interhelical salt bridges between Glu20 and Lys15' and between Glu22 and Lys27'. 13C-nuclear magnetic resonance measurements of the glutamic acid pKa values at physiological ionic strength indicate that the salt bridge involving Glu22 does not contribute to stability and that the salt bridge involving Glu20 is unfavorable, relative to the corresponding situation with a neutral (protonated) Glu residue. Moreover, the substitution of Glu20 by glutamine is stabilizing. Thus, salt bridges will not necessarily contribute favorably to bZIP dimerization specificity and may indeed be unfavorable, relative to alternative neutral-charge interactions.


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