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The X-ray structure of the GCN4-bZIP bound to ATF/CREB site DNA shows the complex depends on DNA flexibility.
J Mol Biol. 1993 Sep 05; 233(1):139-54.JM

Abstract

The X-ray structure of the DNA binding domain of the yeast transcriptional activator protein GCN4 bound to a DNA fragment containing the sequence of the perfectly symmetrical ATF/CREB site has been solved to 3.0 A resolution. The architecture of this specific recognition complex supports the current model for bZIP proteins: a homodimer of parallel alpha-helices form an interhelix coiled-coil region via the leucine zipper, and the two N-terminal basic regions fit into the major groove of half sites on opposite sides of the DNA double helix. The structure shows that DNA flexibility plays the predominant role in the preservation of protein contacts with the symmetric ATF/CREB site (ATGACGTCAT) as compared to the pseudo-symmetric AP-1 target site (ATGACTCAT), overcoming the positional displacement of functional groups introduced by the additional G.C base-pair at the center of the ATF/CREB sequence.

Authors+Show Affiliations

Institut für Molekularbiologie und Biophysik ETH-Höngerberg, Zürich, Switzerland.No affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

8377181

Citation

König, P, and T J. Richmond. "The X-ray Structure of the GCN4-bZIP Bound to ATF/CREB Site DNA Shows the Complex Depends On DNA Flexibility." Journal of Molecular Biology, vol. 233, no. 1, 1993, pp. 139-54.
König P, Richmond TJ. The X-ray structure of the GCN4-bZIP bound to ATF/CREB site DNA shows the complex depends on DNA flexibility. J Mol Biol. 1993;233(1):139-54.
König, P., & Richmond, T. J. (1993). The X-ray structure of the GCN4-bZIP bound to ATF/CREB site DNA shows the complex depends on DNA flexibility. Journal of Molecular Biology, 233(1), 139-54.
König P, Richmond TJ. The X-ray Structure of the GCN4-bZIP Bound to ATF/CREB Site DNA Shows the Complex Depends On DNA Flexibility. J Mol Biol. 1993 Sep 5;233(1):139-54. PubMed PMID: 8377181.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - The X-ray structure of the GCN4-bZIP bound to ATF/CREB site DNA shows the complex depends on DNA flexibility. AU - König,P, AU - Richmond,T J, PY - 1993/9/5/pubmed PY - 1993/9/5/medline PY - 1993/9/5/entrez SP - 139 EP - 54 JF - Journal of molecular biology JO - J Mol Biol VL - 233 IS - 1 N2 - The X-ray structure of the DNA binding domain of the yeast transcriptional activator protein GCN4 bound to a DNA fragment containing the sequence of the perfectly symmetrical ATF/CREB site has been solved to 3.0 A resolution. The architecture of this specific recognition complex supports the current model for bZIP proteins: a homodimer of parallel alpha-helices form an interhelix coiled-coil region via the leucine zipper, and the two N-terminal basic regions fit into the major groove of half sites on opposite sides of the DNA double helix. The structure shows that DNA flexibility plays the predominant role in the preservation of protein contacts with the symmetric ATF/CREB site (ATGACGTCAT) as compared to the pseudo-symmetric AP-1 target site (ATGACTCAT), overcoming the positional displacement of functional groups introduced by the additional G.C base-pair at the center of the ATF/CREB sequence. SN - 0022-2836 UR - https://www.unboundmedicine.com/medline/citation/8377181/The_X_ray_structure_of_the_GCN4_bZIP_bound_to_ATF/CREB_site_DNA_shows_the_complex_depends_on_DNA_flexibility_ DB - PRIME DP - Unbound Medicine ER -