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 Å resolution. Max binds as a dimer to its recognition sequence CACGTG by direct contacts between the α-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 α-helical segments separated by a loop. The two α-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.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 51 print issues and online access
$199.00 per year
only $3.90 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
References
Sun, X.-H. & Baltimore, D. Cell 64, 459–470 (1991).
Murre, C., McCaw, P. S. & Baltimore, D. Cell 56, 777–783 (1989).
Prendergast, G. C. & Ziff, E. B. Nature 341, 392 (1989).
Vinson, C. R., Sigler, P. B. & Mcknight, S. L. Science 246, 911–916 (1989).
Voronova, A. & Baltimore, D. Proc. natn. Acad. Sci. U.S.A. 87, 4722–4726 (1990).
Davis, R. L., Cheng, P.-F., Lassar, A. B. & Weintraub, H. Cell 60, 733–746 (1990).
Fisher, D. E., Parent, L. A. & Sharp, P. A. Cell 72, 467–476 (1993).
Fisher, F. & Goding, C. R. EMBO J. 11, 4103–4109 (1992).
Benezra, R., Davis, R. L., Lockshun, D., Turner, D. L. & Weintraub, H. Cell 61, 49–59 (1990).
Ellis, H. M., Spann, D. R. & Posakony, J. W. Cell 61, 27–38 (1990).
Prendergast, G. C. & Ziff, E. B. Trends Genet. 8, 91–96 (1992).
Torres, R., Schreiber-Agus, N., Morgenbesser, S. D. & DePinho, R. A. Curr. Opin. Cell Biol. 4, 468–474 (1992).
Blackwood, E. & Eisenman, R. N. Science 251, 1211–1217 (1991).
Prendergast, G. C., Lawe, D. & Ziff, E. B. Cell 65, 395–407 (1991).
Blackwood, E., Lüscher, B. & Eisenman, R. N. Genes Dev. 6, 71–80 (1992).
Wenzel, A., Cziepluck, C., Hanann, U., Schumann, J. & Schwab, M. EMBO J. 10, 3703–3712 (1991).
Prendergast, G. C., Hopewell, R., Gorham, B. & Ziff, E. B. Genes Dev. 6, 2429–2439 (1992).
Mukherjee, B., Morgenbesser, S. D. & DePinho, R. A. Genes Dev. 6, 1480–1492 (1992).
Amati, B. et al. Cell 72, 233–245 (1993).
Kato, G., Lee, W. M. F., Chen, L. & Dang, C. Genes Dev. 6, 81–92 (1992).
Littlewood, T. D., Amati, B., Land, H. & Evan, G. I. Oncogene 7, 1783–1792 (1992).
Berberich, S. & Cole, M. D. Genes Dev. 6, 166–172 (1992).
Ayer, D. E., Kretzner, L. & Eisenman, R. N. Cell 72, 211–222 (1993).
Zervos, A. S., Gyuris, J. & Brent, R. Cell 72, 223–232 (1993).
Prendergast, G. C. & Ziff, E. B. Science 251, 186–189 (1991).
DiGabriele, A. D., Sanderson, M. R. & Steitz, T. A. Proc. natn. Acad. Sci. U.S.A. 86, 1816–1820 (1989).
Terwilliger, T. C. & Eisenberg, D. Acta crystallogr. A39, 813–817 (1983).
Zhang, K. Y. J. & Main, P. Acta crystallogr. A46, 377–381 (1990).
Jones, T. A., Zou, J. Y., Cowan, S. W. & Kjeldgaard, M. Acta crystallogr. A47, 110–119 (1991).
Brünger, A. T. X-PLOR v. 3.0 manual (Yale Univ., New Haven, 1992).
Kabsch, W., Mannherz, H. G., Suck, D., Pai, E. F. & Holmes, K. C. Nature 347, 37–44 (1990).
Brünger, A. T., Kuriyan, J. & Karplus, M. Science 235, 458–460 (1987).
Ramachandran, G. N., Ramakrishnan, C. & Sasisekharan, V. J. molec. Biol. 7, 95–99 (1963).
Ellenberger, T. E., Brandl, C. J., Struhl, K. & Harrison, S. C. Cell 71, 1223–1237 (1992).
O'Shea, E. K., Klemm, J. D., Kim, P. S. & Alber, T. Science 254, 539–544 (1991).
Dickerson, R. E. et al. EMBO J. 8, 1–4 (1989).
Wechsler, D. S. & Dang, C. V. Proc. natn. Acad. Sci. U.S.A. 89, 7635–7639 (1992).
Fisher, D. E., Parent, L. A. & Sharp, P. A. Proc. natn. Acad. Sci. U.S.A. 89, 11779–11783 (1992).
Anthony-Cahill, S. J. et al. Science 255, 979–983 (1992).
Vinson, C. R. & Garcia, K. C. New Biol. 4, 396–403 (1992).
Halazonetis, T. D. & Kandil, A. N. Science 255, 464–466 (1992).
Davis, L. J. & Halazonetis, T. D. Oncogene 8, 125–132 (1993).
Starovasnik, M. A., Blackwell, T. K., Laue, T. M., Weintraub, H. & Klevit, R. E. Biochemistry 31, 9891–9903 (1992).
Cai, M. & Davis, R. W. Cell 61, 434–446 (1990).
Halazonetis, T. D. & Kandil, A. N. Proc. natn. Acad. Sci. U.S.A. 88, 6162–6166 (1991).
Blackwell, T. K. & Weintraub, H. Science 250, 1104–1110 (1990).
Blackwell, T. K., Kretzner, L., Blackwood, E. M., Eisenman, R. N. & Weintraub, H. Science 250, 1149–1152 (1990).
Fisher, F., Jayaraman, P.-S. & Goding, C. R. Oncogene 6, 1099–1104 (1991).
Kerkhoff, E., Bister, K. & Klempnauer, K.-H. Proc. natn. Acad. Sci. U.S.A. 88, 4323–4327 (1991).
Dang, C. V., Dolde, C., Gillison, M. L. & Kato, G. J. Proc. natn. Acad. Sci. U.S.A. 89, 599–602 (1992).
Blanar, M. A. & Rutter, W. J. Science 256, 1014–1018 (1992).
Bengal, E. et al. Cell 68, 507–519 (1992).
Studier, F. W., Rosenberg, A. H., Dunn, J. J. & Dubendorff, J. W. Meth. Enzym. 185, 60–89 (1990).
Burgess, R. R. Meth. Enzym. 208, 3–10 (1991).
Chait, B. T. & Kent, S. B. H. Science 257, 1885–1894 (1992).
Puglisi, J. D. & Tinoco, I. Jr Meth. Enzym. 180A, 304–325 (1989).
Finkelstein, K. D. Rev. Sci. Instrum. 63, 305–308 (1992).
Bernstein, F. C. et al. J. molec. Biol. 112, 535–542 (1977).
Gregor, P. D., Sawadogo, M. & Roeder, R. G. Genes Dev. 4, 1730–1740 (1990).
Hu, Y.-F., Lüscher, B., Admon, A., Mermod, N. & Tjian, R. Genes Dev. 4, 1741–1752 (1990).
Beckmann, H., Su, L.-K. & Kadesch, T. Genes Dev. 4, 167–179 (1990).
Carr, C. S. & Sharp, P. A. Molec. cell. Biol. 10, 4384–4388 (1990).
Lassar, A. B. et al. Cell 58, 823–831 (1989).
Richardson, J. S. Meth. Enzym. 115, 359–390 (1985).
Kraulis, P. J. J. appl. Crystallogr. 24, 946–950 (1991).
Anderson, J., Ptashne, M. & Harrison, S. C. Proc. natn. Acad. Sci. U.S.A. 81, 1307–1311 (1984).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Ferré-D'Amaré, A., Prendergast, G., Ziff, E. et al. Recognition by Max of its cognate DNA through a dimeric b/HLH/Z domain. Nature 363, 38–45 (1993). https://doi.org/10.1038/363038a0
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1038/363038a0
This article is cited by
-
Automatic annotation of the bHLH gene family in plants
BMC Genomics (2023)
-
Computational insights into the differentiated binding affinities of Myc, Max, and Omomyc dimers to the E-boxes of DNA
Journal of Molecular Modeling (2022)
-
Comparative analysis of compound NSC13728 as Omomyc homodimer stabilizer by molecular dynamics simulation and MM/GBSA free energy calculation
Journal of Molecular Modeling (2022)
-
Structural and functional organization of the MYC transcriptional factors in Camellia sinensis
Planta (2021)
-
Overexpression of bHLH domain of HIF-1 failed to inhibit the HIF-1 transcriptional activity in hypoxia
Biological Research (2020)
Comments
By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.