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Recognition by Max of its cognate DNA through a dimeric b/HLH/Z domain.
Nature. 1993 May 06; 363(6424):38-45.Nat

Abstract

The three-dimensional structure of the basic/helix-loop-helix/leucine zipper domain of the transcription factor Max complexed with DNA has been determined by X-ray crystallography at 2.9 A resolution. Max binds as a dimer to its recognition sequence CACGTG by direct contacts between the alpha-helical basic region and the major groove. This symmetric homodimer, a new protein fold, is a parallel, left-handed, four-helix bundle, with each monomer containing two alpha-helical segments separated by a loop. The two alpha-helical segments are composed of the basic region plus helix 1 and helix 2 plus the leucine repeat, respectively. As in GCN4, the leucine repeat forms a parallel coiled coil.

Authors+Show Affiliations

Ferré-D'Amaré AR
Laboratories of Molecular Biophysics, Rockefeller University, New York, New York 10021.
Prendergast GC
No affiliation info available
Ziff EB
No affiliation info available
Burley SK
No affiliation info available

MeSH

Amino Acid SequenceAnimalsBase SequenceBasic Helix-Loop-Helix Leucine Zipper Transcription FactorsBasic-Leucine Zipper Transcription FactorsCloning, MolecularComputer SimulationDNADNA-Binding ProteinsEscherichia coliLeucine ZippersMacromolecular SubstancesMiceModels, MolecularMolecular Sequence DataNucleic Acid ConformationProtein BindingProto-Oncogene Proteins c-mycTranscription FactorsX-Ray Diffraction

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

8479534

Citation

Ferré-D'Amaré, A R., et al. "Recognition By Max of Its Cognate DNA Through a Dimeric b/HLH/Z Domain." Nature, vol. 363, no. 6424, 1993, pp. 38-45.
Ferré-D'Amaré AR, Prendergast GC, Ziff EB, et al. Recognition by Max of its cognate DNA through a dimeric b/HLH/Z domain. Nature. 1993;363(6424):38-45.
Ferré-D'Amaré, A. R., Prendergast, G. C., Ziff, E. B., & Burley, S. K. (1993). Recognition by Max of its cognate DNA through a dimeric b/HLH/Z domain. Nature, 363(6424), 38-45.
Ferré-D'Amaré AR, et al. Recognition By Max of Its Cognate DNA Through a Dimeric b/HLH/Z Domain. Nature. 1993 May 6;363(6424):38-45. PubMed PMID: 8479534.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Recognition by Max of its cognate DNA through a dimeric b/HLH/Z domain. AU - Ferré-D'Amaré,A R, AU - Prendergast,G C, AU - Ziff,E B, AU - Burley,S K, PY - 1993/5/6/pubmed PY - 1993/5/6/medline PY - 1993/5/6/entrez SP - 38 EP - 45 JF - Nature JO - Nature VL - 363 IS - 6424 N2 - The three-dimensional structure of the basic/helix-loop-helix/leucine zipper domain of the transcription factor Max complexed with DNA has been determined by X-ray crystallography at 2.9 A resolution. Max binds as a dimer to its recognition sequence CACGTG by direct contacts between the alpha-helical basic region and the major groove. This symmetric homodimer, a new protein fold, is a parallel, left-handed, four-helix bundle, with each monomer containing two alpha-helical segments separated by a loop. The two alpha-helical segments are composed of the basic region plus helix 1 and helix 2 plus the leucine repeat, respectively. As in GCN4, the leucine repeat forms a parallel coiled coil. SN - 0028-0836 UR - https://www.unboundmedicine.com/medline/citation/8479534/Recognition_by_Max_of_its_cognate_DNA_through_a_dimeric_b/HLH/Z_domain_ L2 - https://doi.org/10.1038/363038a0 DB - PRIME DP - Unbound Medicine ER -