1YGH
 
 | | HAT DOMAIN OF GCN5 FROM SACCHAROMYCES CEREVISIAE | | 分子名称: | GLYCEROL, PROTEIN (TRANSCRIPTIONAL ACTIVATOR GCN5) | | 著者 | Trievel, R.C, Rojas, J.R, Sterner, D.E, Venkataramani, R, Wang, L, Zhou, J, Allis, C.D, Berger, S.L, Marmorstein, R. | | 登録日 | 1999-05-27 | | 公開日 | 1999-08-02 | | 最終更新日 | 2024-04-03 | | 実験手法 | X-RAY DIFFRACTION (1.9 Å) | | 主引用文献 | Crystal structure and mechanism of histone acetylation of the yeast GCN5 transcriptional coactivator.
Proc.Natl.Acad.Sci.USA, 96, 1999
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5GCN
 | | CATALYTIC DOMAIN OF TETRAHYMENA GCN5 HISTONE ACETYLTRANSFERASE IN COMPLEX WITH COENZYME A | | 分子名称: | COENZYME A, HISTONE ACETYLTRANSFERASE GCN5 | | 著者 | Lin, Y, Fletcher, C.M, Zhou, J, Allis, C.D, Wagner, G. | | 登録日 | 1999-03-24 | | 公開日 | 1999-07-19 | | 最終更新日 | 2024-05-22 | | 実験手法 | SOLUTION NMR | | 主引用文献 | Solution structure of the catalytic domain of GCN5 histone acetyltransferase bound to coenzyme A
Nature, 400, 1999
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1PDQ
 | | Polycomb chromodomain complexed with the histone H3 tail containing trimethyllysine 27. | | 分子名称: | Histone H3.3, Polycomb protein | | 著者 | Fischle, W, Wang, Y, Jacobs, S.A, Kim, Y, Allis, C.D, Khorasanizadeh, S. | | 登録日 | 2003-05-20 | | 公開日 | 2003-08-26 | | 最終更新日 | 2023-08-16 | | 実験手法 | X-RAY DIFFRACTION (1.76 Å) | | 主引用文献 | Molecular basis for the discrimination of repressive methyl-lysine marks in histone H3 by Polycomb and HP1 chromodomains
Genes Dev., 17, 2003
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2CNX
 | | WDR5 and Histone H3 Lysine 4 dimethyl complex at 2.1 angstrom | | 分子名称: | HISTONE H3 DIMETHYL-LYSINE 4, WD-REPEAT PROTEIN 5 | | 著者 | Ruthenburg, A.J, Wang, W, Graybosch, D.M, Li, H, Allis, C.D, Patel, D.J, Verdine, G.L. | | 登録日 | 2006-05-25 | | 公開日 | 2006-07-03 | | 最終更新日 | 2023-12-13 | | 実験手法 | X-RAY DIFFRACTION (2.1 Å) | | 主引用文献 | Histone H3 Recognition and Presentation by the Wdr5 Module of the Mll1 Complex
Nat.Struct.Mol.Biol., 13, 2006
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2CO0
 | | WDR5 and unmodified Histone H3 complex at 2.25 Angstrom | | 分子名称: | HISTONE H3 DIMETHYL-LYSINE 4, WD-REPEAT PROTEIN 5 | | 著者 | Ruthenburg, A.J, Wang, W, Graybosch, D.M, Li, H, Allis, C.D, Patel, D.J, Verdine, G.L. | | 登録日 | 2006-05-25 | | 公開日 | 2006-07-03 | | 最終更新日 | 2023-12-13 | | 実験手法 | X-RAY DIFFRACTION (2.25 Å) | | 主引用文献 | Histone H3 Recognition and Presentation by the Wdr5 Module of the Mll1 Complex
Nat.Struct.Mol.Biol., 13, 2006
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2H6Q
 | | Histone H3 recognition and presentation by the WDR5 module of the MLL1 complex | | 分子名称: | Histone H3 K4-Me3 9-residue peptide, WD-repeat protein 5 | | 著者 | Ruthenburg, A.J, Wang, W.-K, Graybosch, D.M, Li, H, Allis, C.D, Patel, D.J, Verdine, G.L. | | 登録日 | 2006-06-01 | | 公開日 | 2006-07-04 | | 最終更新日 | 2023-08-30 | | 実験手法 | X-RAY DIFFRACTION (1.87 Å) | | 主引用文献 | Histone H3 recognition and presentation by the WDR5 module of the MLL1 complex.
Nat.Struct.Mol.Biol., 13, 2006
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2JMJ
 | | NMR solution structure of the PHD domain from the yeast YNG1 protein in complex with H3(1-9)K4me3 peptide | | 分子名称: | Histone H3, Protein YNG1, ZINC ION | | 著者 | Ilin, S, Taverna, S.D, Rogers, R.S, Tanny, J.C, Lavender, H, Li, H, Baker, L, Boyle, J, Blair, L.P, Chait, B.T, Patel, D.J, Aitchison, J.D, Tackett, A.J, Allis, C.D. | | 登録日 | 2006-11-15 | | 公開日 | 2007-07-03 | | 最終更新日 | 2023-12-20 | | 実験手法 | SOLUTION NMR | | 主引用文献 | Yng1 PHD finger binding to H3 trimethylated at K4 promotes NuA3 HAT activity at K14 of H3 and transcription at a subset of targeted ORFs
Mol.Cell, 24, 2006
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2JMI
 | | NMR solution structure of PHD finger fragment of Yeast Yng1 protein in free state | | 分子名称: | Protein YNG1, ZINC ION | | 著者 | Ilin, S, Taverna, S.D, Rogers, R.S, Tanny, J.C, Lavender, H, Li, H, Baker, L, Boyle, J, Blair, L.P, Chait, B.T, Patel, D.J, Aitchison, J.D, Tackett, A.J, Allis, C.D. | | 登録日 | 2006-11-15 | | 公開日 | 2007-07-03 | | 最終更新日 | 2023-12-20 | | 実験手法 | SOLUTION NMR | | 主引用文献 | Yng1 PHD finger binding to H3 trimethylated at K4 promotes NuA3 HAT activity at K14 of H3 and transcription at a subset of targeted ORFs
Mol.Cell, 24, 2006
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2H6N
 | | Histone H3 recognition and presentation by the WDR5 module of the MLL1 complex | | 分子名称: | Histone H3 K4-Me2 9-residue peptide, WD-repeat protein 5 | | 著者 | Ruthenburg, A.J, Wang, W.-K, Graybosch, D.M, Li, H, Allis, C.D, Patel, D.J, Verdine, G.L. | | 登録日 | 2006-05-31 | | 公開日 | 2006-07-04 | | 最終更新日 | 2023-08-30 | | 実験手法 | X-RAY DIFFRACTION (1.5 Å) | | 主引用文献 | Histone H3 recognition and presentation by the WDR5 module of the MLL1 complex.
Nat.Struct.Mol.Biol., 13, 2006
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2H68
 | | Histone H3 recognition and presentation by the WDR5 module of the MLL1 complex | | 分子名称: | WD-repeat protein 5 | | 著者 | Ruthenburg, A.J, Wang, W.-K, Graybosch, D.M, Li, H, Allis, C.D, Patel, D.J, Verdine, G.L. | | 登録日 | 2006-05-30 | | 公開日 | 2006-07-04 | | 最終更新日 | 2023-08-30 | | 実験手法 | X-RAY DIFFRACTION (1.79 Å) | | 主引用文献 | Histone H3 recognition and presentation by the WDR5 module of the MLL1 complex.
Nat.Struct.Mol.Biol., 13, 2006
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2H6K
 | | Histone H3 recognition and presentation by the WDR5 module of the MLL1 complex | | 分子名称: | Histone H3 K4-Me 9-residue peptide, WD-repeat protein 5 | | 著者 | Ruthenburg, A.J, Wang, W.-K, Graybosch, D.M, Li, H, Allis, C.D, Patel, D.J, Verdine, G.L. | | 登録日 | 2006-05-31 | | 公開日 | 2006-07-04 | | 最終更新日 | 2023-08-30 | | 実験手法 | X-RAY DIFFRACTION (1.89 Å) | | 主引用文献 | Histone H3 recognition and presentation by the WDR5 module of the MLL1 complex.
Nat.Struct.Mol.Biol., 13, 2006
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5YYF
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2FSA
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2FUI
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2FUU
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4W5A
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3GL6
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5B79
 | | Crystal structure of DPF2 double PHD finger | | 分子名称: | ZINC ION, Zinc finger protein ubi-d4 | | 著者 | Li, H, Xiong, X. | | 登録日 | 2016-06-05 | | 公開日 | 2016-10-26 | | 最終更新日 | 2023-11-08 | | 実験手法 | X-RAY DIFFRACTION (2.601 Å) | | 主引用文献 | Selective recognition of histone crotonylation by double PHD fingers of MOZ and DPF2
Nat.Chem.Biol., 12, 2016
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6J9J
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5JLE
 | | Crystal structure of SETD2 bound to SAH | | 分子名称: | Histone-lysine N-methyltransferase SETD2, S-ADENOSYL-L-HOMOCYSTEINE, ZINC ION | | 著者 | Li, H, Yang, S, Zheng, X. | | 登録日 | 2016-04-27 | | 公開日 | 2016-11-02 | | 最終更新日 | 2023-11-08 | | 実験手法 | X-RAY DIFFRACTION (2.4 Å) | | 主引用文献 | Molecular basis for oncohistone H3 recognition by SETD2 methyltransferase
Genes Dev., 30, 2016
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5J9S
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5JHN
 | | Structure of G9a SET-domain with Histone H3K9Ala mutant peptide and bound S-adenosylmethionine | | 分子名称: | Histone H3.1 peptide with K9A mutation, Histone-lysine N-methyltransferase EHMT2, S-ADENOSYLMETHIONINE, ... | | 著者 | Jayaram, H, Bellon, S.F, Poy, F. | | 登録日 | 2016-04-21 | | 公開日 | 2016-07-06 | | 最終更新日 | 2024-03-06 | | 実験手法 | X-RAY DIFFRACTION (1.67 Å) | | 主引用文献 | S-adenosyl methionine is necessary for inhibition of the methyltransferase G9a by the lysine 9 to methionine mutation on histone H3.
Proc.Natl.Acad.Sci.USA, 113, 2016
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5JIY
 | | Structure of G9a SET-domain with Histone H3K9norLeucine mutant peptide and bound S-adenosylmethionine | | 分子名称: | Histone H3.1 mutant peptide with H3K9nor-leucine, Histone-lysine N-methyltransferase EHMT2, S-ADENOSYLMETHIONINE, ... | | 著者 | Jayaram, H, Bellon, S.F, Poy, F. | | 登録日 | 2016-04-22 | | 公開日 | 2016-09-14 | | 最終更新日 | 2023-11-15 | | 実験手法 | X-RAY DIFFRACTION (1.48 Å) | | 主引用文献 | S-adenosyl methionine is necessary for inhibition of the methyltransferase G9a by the lysine 9 to methionine mutation on histone H3.
Proc.Natl.Acad.Sci.USA, 113, 2016
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5JJY
 | | Crystal structure of SETD2 bound to histone H3.3 K36M peptide | | 分子名称: | Histone H3.3, Histone-lysine N-methyltransferase SETD2, S-ADENOSYL-L-HOMOCYSTEINE, ... | | 著者 | Yang, S, Zheng, X, Li, H. | | 登録日 | 2016-04-25 | | 公開日 | 2016-11-02 | | 最終更新日 | 2024-04-03 | | 実験手法 | X-RAY DIFFRACTION (2.053 Å) | | 主引用文献 | Molecular basis for oncohistone H3 recognition by SETD2 methyltransferase
Genes Dev., 30, 2016
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5JIN
 | | Structure of G9a SET-domain with Histone H3K9M mutant peptide and bound S-adenosylmethionine | | 分子名称: | Histone H3.1 peptide with K9M mutation, Histone-lysine N-methyltransferase EHMT2, S-ADENOSYLMETHIONINE, ... | | 著者 | Jayaram, H, Bellon, S.F, Poy, F. | | 登録日 | 2016-04-22 | | 公開日 | 2016-07-06 | | 最終更新日 | 2023-09-27 | | 実験手法 | X-RAY DIFFRACTION (1.85 Å) | | 主引用文献 | S-adenosyl methionine is necessary for inhibition of the methyltransferase G9a by the lysine 9 to methionine mutation on histone H3.
Proc.Natl.Acad.Sci.USA, 113, 2016
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