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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

Laboratories of Molecular Biophysics, Rockefeller University, New York, New York 10021.No affiliation info availableNo affiliation info availableNo affiliation info available

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 -