Cited by 269Protein Structure and Dynamicsthermodynamics and calorimetric analysesChemical Synthesis and Analysis

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A thermodynamic scale for leucine zipper stability and dimerization specificity: e and g interhelical interactions.

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Krylov, D., Mikhailenko, I., Vinson, C.·1994·The EMBO Journal

DOI 10.1002/j.1460-2075.1994.tb06579.xPMC PMC395166

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Abstract

The leucine zipper is a dimeric coiled-coil protein structure composed of two amphipathic alpha-helices with the hydrophobic surfaces interacting to create the dimer interface. This structure has been found to mediate the dimerization of two abundant classes of DNA binding proteins: the bZIP and bHLH-Zip proteins. Several workers have reported that amino acids in the e and g positions of the coiled coil can modulate dimerization stability and specificity. Using the bZIP protein VBP as a host molecule, we report a thermodynamic scale (delta delta G) for 27 interhelical interactions in 35 proteins between amino acids in the g and the following e positions (g<==>e') of a leucine zipper coiled coil. We have examined the four commonly occurring amino acids in the e and g positions of bZIP proteins, lysine (K), arginine (R), glutamine (Q), glutamic acid (E), as well as the only other remaining charged amino acid aspartic acid (D), and finally alanine (A) as a reference amino acid. These results indicate that E<==>R is the most stable interhelical pair, being 0.35 kcal/mol more stable than E<==>K. A thermodynamic cycle analysis shows that the E<==>R pair is 1.33 kcal/mol more stable than A<==>A with -1.14 kcal/mol of coupling energy (delta delta Gint) coming from the interaction of E with R. The E<==>K coupling energy is only -0.14 kcal/mol. E interacts with more specificity than Q. The R<==>R pair is less stable than the K<==>K by 0.24 kcal/mol. R interacts with more specificity than K. Q forms more stable pairs with the basic amino acids K and R rather than with E. Changing amino acids in the e position to A creates bZIP proteins that form tetramers.

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Authors: Krylov, D., Mikhailenko, I., & Vinson, C.
Affiliations: National Institutes of Health (US)
Venue: The EMBO Journal
Publisher: Springer Science and Business Media LLC
Published: 1994-06-01
Volume: 13
Issue: 12
Pages: 2849-2861
ISSN: 0261-4189 (ISSN-L)
1460-2075
DOI: 10.1002/j.1460-2075.1994.tb06579.x
PMC: PMC395166
OpenAlex: W2301031628
Semantic Scholar: e223136a6090aa7f84312e0d6991cd8cf28a68c5
Cited by: 269
References: 68
Citations by year: 2026: 2 · 2025: 6 · 2024: 3 · 2023: 1 · 2022: 6 · 2021: 6 · 2020: 6 · 2019: 9 · 2018: 2 · 2017: 4 · 2016: 3 · 2015: 8 · 2014: 12 · 2013: 7 · 2012: 11
FWCI: 5.57
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
Locations: The EMBO Journal (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health
National Center for Research Resources (RR 04328, P41RR004328)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Physical Sciences › Chemistry › Physical and Theoretical Chemistry › thermodynamics and calorimetric analyses
Physical Sciences › Chemistry › Organic Chemistry › Chemical Synthesis and Analysis
Keywords: leucine zipper, coiled coil, interhelical interactions, bZIP transcription factors, thermodynamic cycle analysis, coupling energy, glutamate, L-arginine, lysine, glutamine, tetramer formation, DNA-binding proteins
MeSH terms: Amino Acid Sequence, Carrier Proteins, Centrifugation, Isopycnic, Circular Dichroism, DNA-Binding Proteins, Models, Chemical, Molecular Sequence Data, Protein Denaturation, Recombinant Proteins, Thermodynamics, Transcription Factors, Leucine Zippers, Protein Structure, Tertiary, Helix-Loop-Helix Motifs, Avian Proteins, Basic-Leucine Zipper Transcription Factors, G-Box Binding Factors

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A thermodynamic scale for leucine zipper stability and dimerization specificity: e and g interhelical interactions.

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