(en) B. W. Matthews, D. H. Ohlendorf, W. F. Anderson et Y. Takeda, « Structure of the DNA-binding region of lac repressor inferred from its homology with cro repressor », Proceedings of the National Academy of Sciences of the United States of America, vol. 79, no 5, , p. 1428-1432 (PMID6951187, PMCID345986, DOI10.1073/pnas.79.5.1428, lire en ligne)
(en) W. F. Anderson, D. H. Ohlendorf, Y. Takeda et B. W. Matthews, « Structure of the cro repressor from bacteriophage λ and its interaction with DNA », Nature, vol. 290, no 5809, , p. 754-758 (PMID6452580, DOI10.1038/290754a0, lire en ligne)
(en) David B. McKay et Thomas A. Steitz, « Structure of catabolite gene activator protein at 2.9 Å resolution suggests binding to left-handed B-DNA », Nature, vol. 290, no 5809, , p. 744-749 (PMID6261152, DOI10.1038/290744a0, lire en ligne)
(en) Carl O. Pabo et Mitchell Lewis, « The operator-binding domain of λ repressor: structure and DNA recognition », Nature, vol. 289, no 5873, , p. 443-447 (PMID7088190, DOI10.1038/298443a0, lire en ligne)
(en) René Wintjens et Marianne Rooman, « Structural classification of HTH DNA-binding domains and protein-DNA interaction modes », Journal of Molecular Biology, vol. 262, no 2, , p. 294-313 (PMID8831795, DOI10.1006/jmbi.1996.0514, lire en ligne)
(en) Masashi Suzuki et Steven E. Brenner, « Classification of multi-helical DNA-binding domains and application to predict the DBD structures of σ factor, LysR, OmpR/PhoB, CENP-B, Rap1, and XylS/Ada/AraC », FEBS Letters, vol. 372, nos 2-3, , p. 215-212 (PMID7556672, DOI10.1016/0014-5793(95)00988-L, lire en ligne)
(en) L. Aravind, Vivek Anantharaman, Santhanam Balaji, M. Mohan Babu et Lakshminarayan M. Iyer, « The many faces of the helix-turn-helix domain: Transcription regulation and beyond », FEMS Microbiology Reviews, vol. 29, no 2, , p. 231-262 (PMID15808743, DOI10.1016/j.fmrre.2004.12.008, lire en ligne)
(en) Tomasz L. Religa, Christopher M. Johnson, Dung M. Vu, Scott H. Brewer, R. Brian Dyer et Alan R. Fersht, « The helix–turn–helix motif as an ultrafast independently folding domain: The pathway of folding of Engrailed homeodomain », Proceedings of the National Academy of Sciences of the United States of America, vol. 104, no 22, , p. 9272-9277 (PMID17517666, PMCID1890484, DOI10.1073/pnas.0703434104, lire en ligne)
(en) K. Ogata, H. Hojo, S. Aimoto, T. Nakai, H. Nakamura, A. Sarai, S. Ishii et Y. Nishimura, « Solution structure of a DNA-binding unit of Myb: a helix-turn-helix-related motif with conserved tryptophans forming a hydrophobic core », Proceedings of the National Academy of Sciences of the United States of America, vol. 89, no 14, , p. 6428-6432 (PMID1631139, PMCID49514, DOI10.1073/pnas.89.14.6428, lire en ligne)
(en) W. Hinrichs, C. Kisker, M. Duvel, A. Muller, K. Tovar, W. Hillen et W. Saenger, « Structure of the Tet repressor-tetracycline complex and regulation of antibiotic resistance », Science, vol. 264, no 5157, , p. 418-420 (PMID8153629, DOI10.1126/science.8153629, lire en ligne)
(en) Junji Iwahara et Robert T. Clubb, « Solution structure of the DNA binding domain from Dead ringer, a sequence‐specific AT‐rich interaction domain (ARID) », EMBO Press, vol. 18, no 21, , p. 6084-6094 (PMID10545119, PMCID1171673, DOI10.1093/emboj/18.21.6084, lire en ligne)
(en) Andrew D. Sharrocks, A.Louise Brown, Yan Ling et Paula R. Yates, « The ETS-domain transcription factor family », The International Journal of Biochemistry & Cell Biology, vol. 29, no 12, , p. 1371-1387 (PMID9570133, DOI10.1016/S1357-2725(97)00086-1, lire en ligne)
(en) Michael N. Alekshun, Stuart B. Levy, Tanya R. Mealy, Barbara A. Seaton et James F. Head, « The crystal structure of MarR, a regulator of multiple antibiotic resistance, at 2.3 Å resolution », Nature Structural Biology, vol. 8, no 8, , p. 710-714 (PMID11473263, DOI10.1038/90429, lire en ligne)
embopress.org
emboj.embopress.org
(en) Junji Iwahara et Robert T. Clubb, « Solution structure of the DNA binding domain from Dead ringer, a sequence‐specific AT‐rich interaction domain (ARID) », EMBO Press, vol. 18, no 21, , p. 6084-6094 (PMID10545119, PMCID1171673, DOI10.1093/emboj/18.21.6084, lire en ligne)
jbc.org
(en) R. G. Brennan et B. W. Matthews, « The helix-turn-helix DNA binding motif », Journal of Biological Chemistry, vol. 264, no 4, , p. 1903-1906 (PMID2644244, lire en ligne)
nature.com
(en) W. F. Anderson, D. H. Ohlendorf, Y. Takeda et B. W. Matthews, « Structure of the cro repressor from bacteriophage λ and its interaction with DNA », Nature, vol. 290, no 5809, , p. 754-758 (PMID6452580, DOI10.1038/290754a0, lire en ligne)
(en) David B. McKay et Thomas A. Steitz, « Structure of catabolite gene activator protein at 2.9 Å resolution suggests binding to left-handed B-DNA », Nature, vol. 290, no 5809, , p. 744-749 (PMID6261152, DOI10.1038/290744a0, lire en ligne)
(en) Carl O. Pabo et Mitchell Lewis, « The operator-binding domain of λ repressor: structure and DNA recognition », Nature, vol. 289, no 5873, , p. 443-447 (PMID7088190, DOI10.1038/298443a0, lire en ligne)
(en) Michael N. Alekshun, Stuart B. Levy, Tanya R. Mealy, Barbara A. Seaton et James F. Head, « The crystal structure of MarR, a regulator of multiple antibiotic resistance, at 2.3 Å resolution », Nature Structural Biology, vol. 8, no 8, , p. 710-714 (PMID11473263, DOI10.1038/90429, lire en ligne)
nih.gov
ncbi.nlm.nih.gov
(en) R. G. Brennan et B. W. Matthews, « The helix-turn-helix DNA binding motif », Journal of Biological Chemistry, vol. 264, no 4, , p. 1903-1906 (PMID2644244, lire en ligne)
(en) B. W. Matthews, D. H. Ohlendorf, W. F. Anderson et Y. Takeda, « Structure of the DNA-binding region of lac repressor inferred from its homology with cro repressor », Proceedings of the National Academy of Sciences of the United States of America, vol. 79, no 5, , p. 1428-1432 (PMID6951187, PMCID345986, DOI10.1073/pnas.79.5.1428, lire en ligne)
(en) W. F. Anderson, D. H. Ohlendorf, Y. Takeda et B. W. Matthews, « Structure of the cro repressor from bacteriophage λ and its interaction with DNA », Nature, vol. 290, no 5809, , p. 754-758 (PMID6452580, DOI10.1038/290754a0, lire en ligne)
(en) David B. McKay et Thomas A. Steitz, « Structure of catabolite gene activator protein at 2.9 Å resolution suggests binding to left-handed B-DNA », Nature, vol. 290, no 5809, , p. 744-749 (PMID6261152, DOI10.1038/290744a0, lire en ligne)
(en) Carl O. Pabo et Mitchell Lewis, « The operator-binding domain of λ repressor: structure and DNA recognition », Nature, vol. 289, no 5873, , p. 443-447 (PMID7088190, DOI10.1038/298443a0, lire en ligne)
(en) René Wintjens et Marianne Rooman, « Structural classification of HTH DNA-binding domains and protein-DNA interaction modes », Journal of Molecular Biology, vol. 262, no 2, , p. 294-313 (PMID8831795, DOI10.1006/jmbi.1996.0514, lire en ligne)
(en) Masashi Suzuki et Steven E. Brenner, « Classification of multi-helical DNA-binding domains and application to predict the DBD structures of σ factor, LysR, OmpR/PhoB, CENP-B, Rap1, and XylS/Ada/AraC », FEBS Letters, vol. 372, nos 2-3, , p. 215-212 (PMID7556672, DOI10.1016/0014-5793(95)00988-L, lire en ligne)
(en) L. Aravind, Vivek Anantharaman, Santhanam Balaji, M. Mohan Babu et Lakshminarayan M. Iyer, « The many faces of the helix-turn-helix domain: Transcription regulation and beyond », FEMS Microbiology Reviews, vol. 29, no 2, , p. 231-262 (PMID15808743, DOI10.1016/j.fmrre.2004.12.008, lire en ligne)
(en) Tomasz L. Religa, Christopher M. Johnson, Dung M. Vu, Scott H. Brewer, R. Brian Dyer et Alan R. Fersht, « The helix–turn–helix motif as an ultrafast independently folding domain: The pathway of folding of Engrailed homeodomain », Proceedings of the National Academy of Sciences of the United States of America, vol. 104, no 22, , p. 9272-9277 (PMID17517666, PMCID1890484, DOI10.1073/pnas.0703434104, lire en ligne)
(en) K. Ogata, H. Hojo, S. Aimoto, T. Nakai, H. Nakamura, A. Sarai, S. Ishii et Y. Nishimura, « Solution structure of a DNA-binding unit of Myb: a helix-turn-helix-related motif with conserved tryptophans forming a hydrophobic core », Proceedings of the National Academy of Sciences of the United States of America, vol. 89, no 14, , p. 6428-6432 (PMID1631139, PMCID49514, DOI10.1073/pnas.89.14.6428, lire en ligne)
(en) W. Hinrichs, C. Kisker, M. Duvel, A. Muller, K. Tovar, W. Hillen et W. Saenger, « Structure of the Tet repressor-tetracycline complex and regulation of antibiotic resistance », Science, vol. 264, no 5157, , p. 418-420 (PMID8153629, DOI10.1126/science.8153629, lire en ligne)
(en) Junji Iwahara et Robert T. Clubb, « Solution structure of the DNA binding domain from Dead ringer, a sequence‐specific AT‐rich interaction domain (ARID) », EMBO Press, vol. 18, no 21, , p. 6084-6094 (PMID10545119, PMCID1171673, DOI10.1093/emboj/18.21.6084, lire en ligne)
(en) L. W. Donaldson, J. M. Petersen, B. J. Graves et L. P. McIntosh, « Solution structure of the ETS domain from murine Ets-1: a winged helix-turn-helix DNA binding motif », The EMBO Journal, vol. 15, no 1, , p. 125-134 (PMID8598195, PMCID449924)
(en) Andrew D. Sharrocks, A.Louise Brown, Yan Ling et Paula R. Yates, « The ETS-domain transcription factor family », The International Journal of Biochemistry & Cell Biology, vol. 29, no 12, , p. 1371-1387 (PMID9570133, DOI10.1016/S1357-2725(97)00086-1, lire en ligne)
(en) Michael N. Alekshun, Stuart B. Levy, Tanya R. Mealy, Barbara A. Seaton et James F. Head, « The crystal structure of MarR, a regulator of multiple antibiotic resistance, at 2.3 Å resolution », Nature Structural Biology, vol. 8, no 8, , p. 710-714 (PMID11473263, DOI10.1038/90429, lire en ligne)
pnas.org
(en) B. W. Matthews, D. H. Ohlendorf, W. F. Anderson et Y. Takeda, « Structure of the DNA-binding region of lac repressor inferred from its homology with cro repressor », Proceedings of the National Academy of Sciences of the United States of America, vol. 79, no 5, , p. 1428-1432 (PMID6951187, PMCID345986, DOI10.1073/pnas.79.5.1428, lire en ligne)
(en) Tomasz L. Religa, Christopher M. Johnson, Dung M. Vu, Scott H. Brewer, R. Brian Dyer et Alan R. Fersht, « The helix–turn–helix motif as an ultrafast independently folding domain: The pathway of folding of Engrailed homeodomain », Proceedings of the National Academy of Sciences of the United States of America, vol. 104, no 22, , p. 9272-9277 (PMID17517666, PMCID1890484, DOI10.1073/pnas.0703434104, lire en ligne)
(en) K. Ogata, H. Hojo, S. Aimoto, T. Nakai, H. Nakamura, A. Sarai, S. Ishii et Y. Nishimura, « Solution structure of a DNA-binding unit of Myb: a helix-turn-helix-related motif with conserved tryptophans forming a hydrophobic core », Proceedings of the National Academy of Sciences of the United States of America, vol. 89, no 14, , p. 6428-6432 (PMID1631139, PMCID49514, DOI10.1073/pnas.89.14.6428, lire en ligne)
sciencedirect.com
(en) René Wintjens et Marianne Rooman, « Structural classification of HTH DNA-binding domains and protein-DNA interaction modes », Journal of Molecular Biology, vol. 262, no 2, , p. 294-313 (PMID8831795, DOI10.1006/jmbi.1996.0514, lire en ligne)
(en) Andrew D. Sharrocks, A.Louise Brown, Yan Ling et Paula R. Yates, « The ETS-domain transcription factor family », The International Journal of Biochemistry & Cell Biology, vol. 29, no 12, , p. 1371-1387 (PMID9570133, DOI10.1016/S1357-2725(97)00086-1, lire en ligne)
sciencemag.org
science.sciencemag.org
(en) W. Hinrichs, C. Kisker, M. Duvel, A. Muller, K. Tovar, W. Hillen et W. Saenger, « Structure of the Tet repressor-tetracycline complex and regulation of antibiotic resistance », Science, vol. 264, no 5157, , p. 418-420 (PMID8153629, DOI10.1126/science.8153629, lire en ligne)
wiley.com
onlinelibrary.wiley.com
(en) Masashi Suzuki et Steven E. Brenner, « Classification of multi-helical DNA-binding domains and application to predict the DBD structures of σ factor, LysR, OmpR/PhoB, CENP-B, Rap1, and XylS/Ada/AraC », FEBS Letters, vol. 372, nos 2-3, , p. 215-212 (PMID7556672, DOI10.1016/0014-5793(95)00988-L, lire en ligne)
(en) L. Aravind, Vivek Anantharaman, Santhanam Balaji, M. Mohan Babu et Lakshminarayan M. Iyer, « The many faces of the helix-turn-helix domain: Transcription regulation and beyond », FEMS Microbiology Reviews, vol. 29, no 2, , p. 231-262 (PMID15808743, DOI10.1016/j.fmrre.2004.12.008, lire en ligne)