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Tan, S., & Richmond, T. J. (1998). Crystal structure of the yeast MATα2/MCM1/DNA ternary complex. Nature, 391(6668), 660–666.

Authors 2
  1. Song Tan (first)
  2. Timothy J. Richmond (additional)
References 42 Referenced 183
  1. Gehring, W. J. et al. Homeodomain-DNA recognition. Cell 78, 211–223 (1994). (10.1016/0092-8674(94)90292-5) / Cell by WJ Gehring (1994)
  2. Wilson, D. S. & Desplan, C. Homeodomain proteins. Cooperating to be different. Curr. Biol. 5, 32–34 (1995). (10.1016/S0960-9822(95)00010-8) / Curr. Biol. by DS Wilson (1995)
  3. Wolberger, C. Homeodomain interactions. Curr. Opin. Struct. Biol. 6, 62–68 (1996). (10.1016/S0959-440X(96)80096-0) / Curr. Opin. Struct. Biol. by C Wolberger (1996)
  4. Vershon, A. K. Protein interactions of homeodomain proteins. Curr. Opin. Biotechnol. 7, 392–396 (1996). (10.1016/S0958-1669(96)80113-3) / Curr. Opin. Biotechnol. by AK Vershon (1996)
  5. Johnson, A. D. Molecular mechanisms of cell-type determination in budding yeast. Curr. Opin. Genet. Dev. 5, 552–558 (1995). (10.1016/0959-437X(95)80022-0) / Curr. Opin. Genet. Dev. by AD Johnson (1995)
  6. Sauer, R. T., Smith, D. L. & Johnson, A. D. Flexibility of the yeast alpha 2 repressor enables it to occupy the ends of its operator, leaving the center free. Genes Dev. 2, 807–816 (1988). (10.1101/gad.2.7.807) / Genes Dev. by RT Sauer (1988)
  7. Hall, M. N. & Johnson, A. D. Homeodomain of the yeast repressor alpha 2 is a sequence-specific DNA-binding domain but is not sufficient for repression. Science 237, 1007–1012 (1987). (10.1126/science.2887035) / Science by MN Hall (1987)
  8. Komachi, K., Redd, M. J. & Johnson, A. D. The WD repeats of Tup1 interact with the homeodomain protein alpha 2. Genes Dev. 8, 2857–2867 (1994). (10.1101/gad.8.23.2857) / Genes Dev. by K Komachi (1994)
  9. Wolberger, C., Vershon, A. K., Liu, B., Johnson, A. D. & Pabo, C. O. Crystal structure of a MAT alpha 2 homeodomain–operator complex suggests a general model for homeodomain–DNA interactions. Cell 67, 517–528 (1991). (10.1016/0092-8674(91)90526-5) / Cell by C Wolberger (1991)
  10. Phillips, C. L., Vershon, A. K., Johnson, A. D. & Dahlquist, F. W. Secondary structure of the homeodomain of yeast alpha 2 repressor determined by NMR spectroscopy. Genes. Dev. 5, 764–772 (1991). (10.1101/gad.5.5.764) / Genes. Dev. by CL Phillips (1991)
  11. Mak, A. & Johnson, A. D. The carboxy-terminal tail of the homeodomain protein alpha 2 is required for function with a second homeodomain protein. Genes Dev. 7, 1862–1870 (1993). (10.1101/gad.7.10.1862) / Genes Dev. by A Mak (1993)
  12. Li, T., Stark, M. R., Johnson, A. D. & Wolberger, C. Crystal structure of the MATa1/MAT alpha 2 homeodomain heterodimer bound to DNA. Science 270, 262–269 (1995). (10.1126/science.270.5234.262) / Science by T Li (1995)
  13. Lydall, D., Ammerer, G. & Nasmyth, K. Anew role for MCM1 in yeast: cell cycle regulation of SW15 transcription. Genes Dev. 5, 2405–2519 (1991). (10.1101/gad.5.12b.2405) / Genes Dev. by D Lydall (1991)
  14. Passmore, S., Maine, G. T., Elble, R., Christ, C. & Tye, B. K. Saccharomyces cerevisiae protein involved in plasmid maintenance is necessary for mating of MAT alpha cells. J. Mol. Biol. 204, 593–606 (1988). (10.1016/0022-2836(88)90358-0) / J. Mol. Biol. by S Passmore (1988)
  15. Kuo, M. H., Nadeau, E. T. & Grayhack, E. J. Multiple phosphorylated forms of the Saccharomyces cerevisiae Mcm1 protein include an isoform induced in response to high salt concentrations. Mol. Cell. Biol. 17, 819–832 (1997). (10.1128/MCB.17.2.819) / Mol. Cell. Biol. by MH Kuo (1997)
  16. Althoefer, H., Schleiffer, A., Wassmann, K., Nordheim, A. & Ammerer, G. Mcm1 is required to coordinate G2-specific transcription in Saccharomyces cerevisiae. Mol. Cell. Biol. 15, 5917–5928 (1995). (10.1128/MCB.15.11.5917) / Mol. Cell. Biol. by H Althoefer (1995)
  17. Maher, M., Cong, F., Kindelberger, D., Nasmyth, K. & Dalton, S. Cell cycle-regulated transcription of the CLB2 gene is dependent on Mcm1 and a ternary complex factor. Mol. Cell. Biol. 15, 3129–3137 (1995). (10.1128/MCB.15.6.3129) / Mol. Cell. Biol. by M Maher (1995)
  18. Christ, C. & Tye, B. K. Functional domains of the yeast transcription/replication factor MCM1. Genes Dev. 5, 751–763 (1991). (10.1101/gad.5.5.751) / Genes Dev. by C Christ (1991)
  19. Primig, M., Winkler, H. & Ammerer, G. The DNA binding and oligomerization domain of MCM1 is sufficient for its interaction with other regulatory proteins. EMBO J. 10, 4209–4218 (1991). (10.1002/j.1460-2075.1991.tb04999.x) / EMBO J. by M Primig (1991)
  20. Shore, P. & Sharrocks, A. D. The MADS-box family of transcription factors. Eur. J. Biochem. 229, 1–13 (1995). (10.1111/j.1432-1033.1995.tb20430.x) / Eur. J. Biochem. by P Shore (1995)
  21. Pellegrini, L., Tan, S. & Richmond, T. J. Structure of serum response factor core bound to DNA. Nature 376, 490–498 (1995). (10.1038/376490a0) / Nature by L Pellegrini (1995)
  22. Smith, D. L. & Johnson, A. D. Amolecular mechanism for combinatorial control in yeast: MCM1 protein sets the spacing and orientation of the homeodomains of an alpha 2 dimer. Cell 68, 133–142 (1992). (10.1016/0092-8674(92)90212-U) / Cell by DL Smith (1992)
  23. Vershon, A. K. & Johnson, A. D. Ashort, disordered protein region mediates interactions between the homeodomain of the yeast alpha 2 protein and the MCM1 protein. Cell 72, 105–112 (1993). (10.1016/0092-8674(93)90054-T) / Cell by AK Vershon (1993)
  24. Keleher, C. A., Goutte, C. & Johnson, A. D. The yeast cell-type specific repressor alpha 2 acts cooperatively with a non-cell-type-specific protein. Cell 53, 927–936 (1988). (10.1016/S0092-8674(88)90449-7) / Cell by CA Keleher (1988)
  25. Keleher, C. A., Passmore, S. & Johnson, A. D. Yeast repressor alpha 2 binds to its operator cooperatively with yeast protein Mcm1. Mol. Cell. Biol. 9, 5228–5230 (1989). (10.1128/MCB.9.11.5228) / Mol. Cell. Biol. by CA Keleher (1989)
  26. Mead, J., Zhong, H., Acton, T. B. & Vershon, A. K. The yeast alpha2 and Mcm1 proteins interact through a region similar to a motif found in homeodomain proteins of higher eukaryotes. Mol. Cell. Biol. 16, 2135–2143 (1996). (10.1128/MCB.16.5.2135) / Mol. Cell. Biol. by J Mead (1996)
  27. Minor, D. L. J & Kim, P. S. Context-dependent secondary structure formation of a designed protein sequence. Nature 380, 730–734 (1996). (10.1038/380730a0) / Nature by DLJ Minor (1996)
  28. Wynne, J. & Treisman, R. SRF and MCM1 have related but distinct DNA binding specificities. Nucleic Acids Res. 20, 3297–3303 (1992). (10.1093/nar/20.13.3297) / Nucleic Acids Res. by J Wynne (1992)
  29. Acton, T. B., Zhong, H. & Vershon, A. K. DNA-binding specificity of Mcm1: operator mutations that alter DNA-bending and transcriptional activities by a MADS box protein. Mol. Cell. Biol. 17, 1881–1889 (1997). (10.1128/MCB.17.4.1881) / Mol. Cell. Biol. by TB Acton (1997)
  30. Zhong, H. L. & Vershon, A. K. The yeast homeodomain protein Mat alpha 2 shows extended DNA binding specificity in complex with Mcm1. J. Biol. Chem. 272, 8402–8409 (1997). (10.1074/jbc.272.13.8402) / J. Biol. Chem. by HL Zhong (1997)
  31. Labeots, L. A. & Weiss, M. A. Electrostatics and hydration at the homeodomain DNA interface: chemical probes of an interfacial water cavity. J. Mol. Biol. 269, 113–128 (1997). (10.1006/jmbi.1997.1026) / J. Mol. Biol. by LA Labeots (1997)
  32. Bruhn, L. & Sprague, G. F. J MCM1 point mutants deficient in expression of alpha-specific genes: residues important for interaction with alpha 1. Mol. Cell. Biol. 14, 2534–2544 (1994). (10.1128/MCB.14.4.2534) / Mol. Cell. Biol. by L Bruhn (1994)
  33. Abel, K., Yoder, M. D., Hilgenfeld, R. & Jurnak, F. An alpha to beta conformational switch in EF-Tu. Structure 4, 1153–1159 (1996). (10.1016/S0969-2126(96)00123-2) / Structure by K Abel (1996)
  34. Polekhina, G. et al. Helix unwinding in the effector region of elongation factor EF-Tu–GDP. Structure 4, 1141–1151 (1996). (10.1016/S0969-2126(96)00122-0) / Structure by G Polekhina (1996)
  35. Wright, H. T. The structural puzzle of how serpin serine proteinase inhibitors work. BioEssays 18, 453–464 (1996). (10.1002/bies.950180607) / BioEssays by HT Wright (1996)
  36. Perutz, M. F. Amyloid fibrils. Mutations make enzyme polymerize. Nature 385, 773–775 (1997). (10.1038/385773a0) / Nature by MF Perutz (1997)
  37. Navaza, J. AMoRe: an automated package for molecular replacement. Acta Crystallogr. A 50, 157–163 (1994). (10.1107/S0108767393007597) / Acta Crystallogr. A by J Navaza (1994)
  38. Brünger, A. X-PLOR v3.1 Manual(Yale Univ. Press, New Haven, CT, (1992)).
  39. Tronrud, D. E. Conjugate-direction minimization: an improved method for the refinement of macromolecules. Acta Crystallogr. A 48, 912–916 (1992). (10.1107/S0108767392005415) / Acta Crystallogr. A by DE Tronrud (1992)
  40. Ferrin, T. E., Huang, C. C., Jarvis, L. E. & Langridge, R. The MIDAS display system. J. Mol. Graph. 6, 13–27 (1988). (10.1016/0263-7855(88)80054-7) / J. Mol. Graph. by TE Ferrin (1988)
  41. Lavery, R. & Sklenar, H. The definition of generalised helicoidal parameters and of axis curvature for irregular nucleic acids. J. Biomol. Struct. Dynam. 6, 63–91 (1988). (10.1080/07391102.1988.10506483) / J. Biomol. Struct. Dynam. by R Lavery (1988)
  42. Nicholls, A., Sharp, K. & Honig, B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11, 281–296 (1991). (10.1002/prot.340110407) / Proteins by A Nicholls (1991)
Dates
Type When
Created 23 years ago (July 26, 2002, 4:37 a.m.)
Deposited 2 years, 3 months ago (May 16, 2023, 9:59 p.m.)
Indexed 2 hours, 47 minutes ago (Aug. 24, 2025, 4:50 a.m.)
Issued 27 years, 6 months ago (Feb. 1, 1998)
Published 27 years, 6 months ago (Feb. 1, 1998)
Published Online 27 years, 6 months ago (Feb. 12, 1998)
Published Print 27 years, 6 months ago (Feb. 1, 1998)
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@article{Tan_1998, title={Crystal structure of the yeast MATα2/MCM1/DNA ternary complex}, volume={391}, ISSN={1476-4687}, url={http://dx.doi.org/10.1038/35563}, DOI={10.1038/35563}, number={6668}, journal={Nature}, publisher={Springer Science and Business Media LLC}, author={Tan, Song and Richmond, Timothy J.}, year={1998}, month=feb, pages={660–666} }