doi: 10.1038/363038a0.
Recognition by Max of its cognate DNA through a dimeric b/HLH/Z domain
Affiliations
- PMID: 8479534
- DOI: 10.1038/363038a0
Item in Clipboard
Recognition by Max of its cognate DNA through a dimeric b/HLH/Z domain
Nature.
.
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.
Comment in
-
Structural biology. Max in a complex affair.Nature. 1993 May 6;363(6424):20-1. doi: 10.1038/363020a0. Nature. 1993. PMID: 8479531 No abstract available.
Similar articles
-
The NMR solution structure of a mutant of the Max b/HLH/LZ free of DNA: insights into the specific and reversible DNA binding mechanism of dimeric transcription factors.J Mol Biol. 2004 Sep 17;342(3):813-32. doi: 10.1016/j.jmb.2004.07.058. J Mol Biol. 2004. PMID: 15342239
-
Analysis of the Myc and Max interaction specificity with lambda repressor-HLH domain fusions.J Mol Biol. 1995 May 5;248(3):541-50. doi: 10.1006/jmbi.1995.0241. J Mol Biol. 1995. PMID: 7752223
-
Insights into the mechanism of heterodimerization from the 1H-NMR solution structure of the c-Myc-Max heterodimeric leucine zipper.J Mol Biol. 1998 Aug 7;281(1):165-81. doi: 10.1006/jmbi.1998.1914. J Mol Biol. 1998. PMID: 9680483
-
The basic region/helix-loop-helix/leucine zipper domain of Myc proto-oncoproteins: function and regulation.Oncogene. 1999 May 13;18(19):2955-66. doi: 10.1038/sj.onc.1202750. Oncogene. 1999. PMID: 10378692 Review.
-
X-ray crystallographic studies of eukaryotic transcription initiation factors.Philos Trans R Soc Lond B Biol Sci. 1996 Apr 29;351(1339):483-9. doi: 10.1098/rstb.1996.0046. Philos Trans R Soc Lond B Biol Sci. 1996. PMID: 8735270 Review.
Cited by
-
A transcriptional activator from Rhizophagus irregularis regulates phosphate uptake and homeostasis in AM symbiosis during phosphorous starvation.Front Microbiol. 2023 Jan 20;13:1114089. doi: 10.3389/fmicb.2022.1114089. eCollection 2022. Front Microbiol. 2023. PMID: 36741887 Free PMC article.
-
Mitochondria-to-nuclear signaling is regulated by the subcellular localization of the transcription factors Rtg1p and Rtg3p.Mol Biol Cell. 2000 Jun;11(6):2103-15. doi: 10.1091/mbc.11.6.2103. Mol Biol Cell. 2000. PMID: 10848632 Free PMC article.
-
Using a structural and logics systems approach to infer bHLH-DNA binding specificity determinants.Nucleic Acids Res. 2011 Jun;39(11):4553-63. doi: 10.1093/nar/gkr070. Epub 2011 Feb 18. Nucleic Acids Res. 2011. PMID: 21335608 Free PMC article.
-
Functional interactions among members of the MAX and MLX transcriptional network during oncogenesis.Biochim Biophys Acta. 2015 May;1849(5):484-500. doi: 10.1016/j.bbagrm.2014.05.016. Epub 2014 May 22. Biochim Biophys Acta. 2015. PMID: 24857747 Free PMC article. Review.
-
Genome-wide identification and characterization of cucumber bHLH family genes and the functional characterization of CsbHLH041 in NaCl and ABA tolerance in Arabidopsis and cucumber.BMC Plant Biol. 2020 Jun 11;20(1):272. doi: 10.1186/s12870-020-02440-1. BMC Plant Biol. 2020. PMID: 32527214 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases
Research Materials
