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PDBsum entry 2gp5
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protein ligands metals Protein-protein interface(s) links
Metal binding protein PDB id
2gp5

 

 

 

 

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Contents
Protein chains
347 a.a. *
Ligands
AKG ×2
Metals
_ZN ×2
FE2 ×2
Waters ×125
* Residue conservation analysis
PDB id:
2gp5
Name: Metal binding protein
Title: Crystal structure of catalytic core domain of jmjd2a complexed with alpha-ketoglutarate
Structure: Jumonji domain-containing protein 2a. Chain: a, b. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: jmjd2a. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.28Å     R-factor:   0.236     R-free:   0.285
Authors: Z.Chen,J.Zang,J.Whetstine,X.Hong,F.Davrazou,T.G.Kutateladze, M.Simpson,S.Dai,J.Hagman,Y.Shi,G.Zhang
Key ref:
Z.Chen et al. (2006). Structural insights into histone demethylation by JMJD2 family members. Cell, 125, 691-702. PubMed id: 16677698 DOI: 10.1016/j.cell.2006.04.024
Date:
16-Apr-06     Release date:   23-May-06    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
O75164  (KDM4A_HUMAN) -  Lysine-specific demethylase 4A from Homo sapiens
Seq:
Struc: 		 
Seq:
Struc: 		 
Seq:
Struc: 		1064 a.a.
347 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class 2: E.C.1.14.11.66  - [histone H3]-trimethyl-L-lysine(9) demethylase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: N6,N6,N6-trimethyl-L-lysyl9-[histone H3] + 2 2-oxoglutarate + 2 O2 = N6-methyl-L-lysyl9-[histone H3] + 2 formaldehyde + 2 succinate + 2 CO2
N(6),N(6),N(6)-trimethyl-L-lysyl(9)-[histone H3]
Bound ligand (Het Group name = AKG)
corresponds exactly 		+ 2 × 2-oxoglutarate
 + 2 × O2
 = N(6)-methyl-L-lysyl(9)-[histone H3]
 + 2 × formaldehyde
 + 2 × succinate
 + 2 × CO2
   Enzyme class 3: E.C.1.14.11.69  - [histone H3]-trimethyl-L-lysine(36) demethylase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: N6,N6,N6-trimethyl-L-lysyl36-[histone H3] + 2 2-oxoglutarate + 2 O2 = N6-methyl-L-lysyl36-[histone H3] + 2 formaldehyde + 2 succinate + 2 CO2
N(6),N(6),N(6)-trimethyl-L-lysyl(36)-[histone H3]
Bound ligand (Het Group name = AKG)
corresponds exactly 		+ 2 × 2-oxoglutarate
 + 2 × O2
 = N(6)-methyl-L-lysyl(36)-[histone H3]
 + 2 × formaldehyde
 + 2 × succinate
 + 2 × CO2
Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
DOI no: 10.1016/j.cell.2006.04.024 Cell 125:691-702 (2006)
PubMed id: 16677698  
 
 
Structural insights into histone demethylation by JMJD2 family members.
Z.Chen, J.Zang, J.Whetstine, X.Hong, F.Davrazou, T.G.Kutateladze, M.Simpson, Q.Mao, C.H.Pan, S.Dai, J.Hagman, K.Hansen, Y.Shi, G.Zhang.
 
  ABSTRACT  
 
Posttranslational modifications of histones regulate chromatin structure and gene expression. Histone demethylases, members of a newly emerging transcription-factor family, remove methyl groups from the lysine residues of the histone tails and thereby regulate the transcriptional activity of target genes. JmjC-domain-containing proteins have been predicted to be demethylases. For example, the JmjC-containing protein JMJD2A has been characterized as a H3-K9me3- and H3-K36me3-specific demethylase. Here, structures of the catalytic-core domain of JMJD2A with and without alpha-ketoglutarate in the presence of Fe2+ have been determined by X-ray crystallography. The structure of the core domain, consisting of the JmjN domain, the JmjC domain, the C-terminal domain, and a zinc-finger motif, revealed the unique elements that form a potential substrate binding pocket. Sited-directed mutagenesis in conjunction with demethylase activity assays allowed us to propose a molecular model for substrate selection by the JMJD2 histone demethylase family.
 
  Selected figure(s)  
 
Figure 3.
Figure 3. The Superposition of c-JMJD2A and FIH
The rotation and translation matrix of the superposition was derived from Dali. The structure of c-JMJD2A is colored green, whereas the FIH structure (PDB ID code 1MZF) is colored yellow. Figure 3 and Figure 4 were made with the RIBBON program (Carson, 1987). Figure 3. The Superposition of c-JMJD2A and FIHThe rotation and translation matrix of the superposition was derived from Dali. The structure of c-JMJD2A is colored green, whereas the FIH structure (PDB ID code 1MZF) is colored yellow. Figure 3 and [3]Figure 4 were made with the RIBBON program ([4]Carson, 1987).
Figure 4.
Figure 4. The Detailed Structures of Individual Domains
(A) The structure of the JmjN domain.
(B) The structure of the C-terminal domain.
(C) The structure of the zinc-finger motif formed by the C-terminal domain and the diverse region from JmjC.
(D) The detailed coordination of the zinc atom. Figure 4. The Detailed Structures of Individual Domains(A) The structure of the JmjN domain.(B) The structure of the C-terminal domain.(C) The structure of the zinc-finger motif formed by the C-terminal domain and the diverse region from JmjC.(D) The detailed coordination of the zinc atom.
 
  The above figures are reprinted by permission from Cell Press: Cell (2006, 125, 691-702) copyright 2006.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21321607 A.J.Bannister, and T.Kouzarides (2011).
Regulation of chromatin by histone modifications.
  Cell Res, 21, 381-395.  
  21141727 A.K.Upadhyay, and X.Cheng (2011).
Dynamics of histone lysine methylation: structures of methyl writers and erasers.
  Prog Drug Res, 67, 107-124.  
20972222 M.Kato, Y.Araiso, A.Noma, A.Nagao, T.Suzuki, R.Ishitani, and O.Nureki (2011).
Crystal structure of a novel JmjC-domain-containing protein, TYW5, involved in tRNA modification.
  Nucleic Acids Res, 39, 1576-1585.
PDB codes: 3al5 3al6
21460794 R.Chowdhury, K.K.Yeoh, Y.M.Tian, L.Hillringhaus, E.A.Bagg, N.R.Rose, I.K.Leung, X.S.Li, E.C.Woon, M.Yang, M.A.McDonough, O.N.King, I.J.Clifton, R.J.Klose, T.D.Claridge, P.J.Ratcliffe, C.J.Schofield, and A.Kawamura (2011).
The oncometabolite 2-hydroxyglutarate inhibits histone lysine demethylases.
  EMBO Rep, 12, 463-469.
PDB codes: 2ybk 2ybp 2ybs 2yc0 2yde
21243713 S.Krishnan, S.Horowitz, and R.C.Trievel (2011).
Structure and function of histone H3 lysine 9 methyltransferases and demethylases.
  Chembiochem, 12, 254-263.  
20084082 C.Huang, Y.Xiang, Y.Wang, X.Li, L.Xu, Z.Zhu, T.Zhang, Q.Zhu, K.Zhang, N.Jing, and C.D.Chen (2010).
Dual-specificity histone demethylase KIAA1718 (KDM7A) regulates neural differentiation through FGF4.
  Cell Res, 20, 154-165.  
19910462 H.Hou, Y.Wang, S.P.Kallgren, J.Thompson, J.R.Yates, and S.Jia (2010).
Histone variant H2A.Z regulates centromere silencing and chromosome segregation in fission yeast.
  J Biol Chem, 285, 1909-1918.  
20478993 I.R.Searle, O.Pontes, C.W.Melnyk, L.M.Smith, and D.C.Baulcombe (2010).
JMJ14, a JmjC domain protein, is required for RNA silencing and cell-to-cell movement of an RNA silencing signal in Arabidopsis.
  Genes Dev, 24, 986-991.  
20498719 K.Reuter, M.Pittelkow, J.Bursy, A.Heine, T.Craan, and E.Bremer (2010).
Synthesis of 5-hydroxyectoine from ectoine: crystal structure of the non-heme iron(II) and 2-oxoglutarate-dependent dioxygenase EctD.
  PLoS One, 5, e10647.
PDB code: 3emr
20692206 L.Dang, S.Jin, and S.M.Su (2010).
IDH mutations in glioma and acute myeloid leukemia.
  Trends Mol Med, 16, 387-397.  
21124823 L.Li, C.Greer, R.N.Eisenman, and J.Secombe (2010).
Essential functions of the histone demethylase lid.
  PLoS Genet, 6, e1001221.  
20423905 L.M.Iyer, S.Abhiman, R.F.de Souza, and L.Aravind (2010).
Origin and evolution of peptide-modifying dioxygenases and identification of the wybutosine hydroxylase/hydroperoxidase.
  Nucleic Acids Res, 38, 5261-5279.  
20101266 L.Yu, Y.Wang, S.Huang, J.Wang, Z.Deng, Q.Zhang, W.Wu, X.Zhang, Z.Liu, W.Gong, and Z.Chen (2010).
Structural insights into a novel histone demethylase PHF8.
  Cell Res, 20, 166-173.
PDB codes: 3k3n 3k3o
20210752 M.L.Bellows, and C.A.Floudas (2010).
Computational methods for de novo protein design and its applications to the human immunodeficiency virus 1, purine nucleoside phosphorylase, ubiquitin specific protease 7, and histone demethylases.
  Curr Drug Targets, 11, 264-278.  
20373914 N.Mosammaparast, and Y.Shi (2010).
Reversal of histone methylation: biochemical and molecular mechanisms of histone demethylases.
  Annu Rev Biochem, 79, 155-179.  
20159995 R.Collins, and X.Cheng (2010).
A case study in cross-talk: the histone lysine methyltransferases G9a and GLP.
  Nucleic Acids Res, 38, 3503-3511.  
21095589 S.A.Miller, S.E.Mohn, and A.S.Weinmann (2010).
Jmjd3 and UTX play a demethylase-independent role in chromatin remodeling to regulate T-box family member-dependent gene expression.
  Mol Cell, 40, 594-605.  
20679243 X.Hong, J.Zang, J.White, C.Wang, C.H.Pan, R.Zhao, R.C.Murphy, S.Dai, P.Henson, J.W.Kappler, J.Hagman, and G.Zhang (2010).
Interaction of JMJD6 with single-stranded RNA.
  Proc Natl Acad Sci U S A, 107, 14568-14572.
PDB codes: 3ld8 3ldb
21067515 Y.Chang, J.Wu, X.J.Tong, J.Q.Zhou, and J.Ding (2010).
Crystal structure of the catalytic core of Saccharomyces cerevesiae histone demethylase Rph1: insights into the substrate specificity and catalytic mechanism.
  Biochem J, 433, 295-302.
PDB codes: 3opt 3opw
20567261 Y.Yang, L.Hu, P.Wang, H.Hou, Y.Lin, Y.Liu, Z.Li, R.Gong, X.Feng, L.Zhou, W.Zhang, Y.Dong, H.Yang, H.Lin, Y.Wang, C.D.Chen, and Y.Xu (2010).
Structural insights into a dual-specificity histone demethylase ceKDM7A from Caenorhabditis elegans.
  Cell Res, 20, 886-898.
PDB codes: 3n9l 3n9m 3n9n 3n9o 3n9p 3n9q
20868382 Y.Yu, A.M.Neiman, and R.Sternglanz (2010).
The JmjC domain of Gis1 is dispensable for transcriptional activation.
  FEMS Yeast Res, 10, 793-801.  
20531378 Z.Zhu, Y.Wang, X.Li, Y.Wang, L.Xu, X.Wang, T.Sun, X.Dong, L.Chen, H.Mao, Y.Yu, J.Li, J.Li, P.A.Chen, and C.D.Chen (2010).
PHF8 is a histone H3K9me2 demethylase regulating rRNA synthesis.
  Cell Res, 20, 794-801.  
18790076 A.Mai, and L.Altucci (2009).
Epi-drugs to fight cancer: from chemistry to cancer treatment, the road ahead.
  Int J Biochem Cell Biol, 41, 199-213.  
19390830 E.H.Hong, Y.M.Jeong, J.Y.Ryu, R.M.Amasino, B.Noh, and Y.S.Noh (2009).
Temporal and spatial expression patterns of nine Arabidopsis genes encoding Jumonji C-domain proteins.
  Mol Cells, 27, 481-490.  
19224247 G.Govind, V.T.Harshavardhan, H.V.ThammeGowda, J.K.Patricia, P.J.Kalaiarasi, R.Dhanalakshmi, D.R.Iyer, M.Senthil Kumar, S.K.Muthappa, N.Sreenivasulu, S.Nese, M.Udayakumar, and U.K.Makarla (2009).
Identification and functional validation of a unique set of drought induced genes preferentially expressed in response to gradual water stress in peanut.
  Mol Genet Genomics, 281, 591-605.  
19096759 H.Chen, and M.Costa (2009).
Iron- and 2-oxoglutarate-dependent dioxygenases: an emerging group of molecular targets for nickel toxicity and carcinogenicity.
  Biometals, 22, 191-196.  
19376846 Q.Li, Q.Ke, and M.Costa (2009).
Alterations of histone modifications by cobalt compounds.
  Carcinogenesis, 30, 1243-1251.  
18923809 S.S.Ng, W.W.Yue, U.Oppermann, and R.J.Klose (2009).
Dynamic protein methylation in chromatin biology.
  Cell Mol Life Sci, 66, 407-422.  
18593478 C.S.Veerappan, Z.Avramova, and E.N.Moriyama (2008).
Evolution of SET-domain protein families in the unicellular and multicellular Ascomycota fungi.
  BMC Evol Biol, 8, 190.  
18713399 F.Lu, G.Li, X.Cui, C.Liu, X.J.Wang, and X.Cao (2008).
Comparative analysis of JmjC domain-containing proteins reveals the potential histone demethylases in Arabidopsis and rice.
  J Integr Plant Biol, 50, 886-896.  
17668288 H.Tan, S.Wu, J.Wang, and Z.K.Zhao (2008).
The JMJD2 members of histone demethylase revisited.
  Mol Biol Rep, 35, 551-556.  
18084306 J.Lee, J.R.Thompson, M.V.Botuyan, and G.Mer (2008).
Distinct binding modes specify the recognition of methylated histones H3K4 and H4K20 by JMJD2A-tudor.
  Nat Struct Mol Biol, 15, 109-111.
PDB codes: 2qqr 2qqs
18813363 J.M.Simmons, T.A.Müller, and R.P.Hausinger (2008).
Fe(II)/alpha-ketoglutarate hydroxylases involved in nucleobase, nucleoside, nucleotide, and chromatin metabolism.
  Dalton Trans, (), 5132-5142.  
18611856 K.S.Hewitson, S.L.Holmes, D.Ehrismann, A.P.Hardy, R.Chowdhury, C.J.Schofield, and M.A.McDonough (2008).
Evidence that two enzyme-derived histidine ligands are sufficient for iron binding and catalysis by factor inhibiting HIF (FIH).
  J Biol Chem, 283, 25971-25978.
PDB codes: 2ilm 3d8c
18375980 M.Lloret-Llinares, C.Carré, A.Vaquero, N.de Olano, and F.Azorín (2008).
Characterization of Drosophila melanogaster JmjC+N histone demethylases.
  Nucleic Acids Res, 36, 2852-2863.  
18564434 P.Hahn, J.Böse, S.Edler, and A.Lengeling (2008).
Genomic structure and expression of Jmjd6 and evolutionary analysis in the context of related JmjC domain containing proteins.
  BMC Genomics, 9, 293.  
18765808 Q.Sun, and D.X.Zhou (2008).
Rice jmjC domain-containing gene JMJ706 encodes H3K9 demethylase required for floral organ development.
  Proc Natl Acad Sci U S A, 105, 13679-13684.  
19075677 X.Wu, and X.Hua (2008).
Menin, histone h3 methyltransferases, and regulation of cell proliferation: current knowledge and perspective.
  Curr Mol Med, 8, 805-815.  
17301803 A.Ozer, and R.K.Bruick (2007).
Non-heme dioxygenases: cellular sensors and regulators jelly rolled into one?
  Nat Chem Biol, 3, 144-153.  
17151105 B.Alberter, and A.Ensser (2007).
Histone modification pattern of the T-cellular Herpesvirus saimiri genome in latency.
  J Virol, 81, 2524-2530.  
17947579 B.Chang, Y.Chen, Y.Zhao, and R.K.Bruick (2007).
JMJD6 is a histone arginine demethylase.
  Science, 318, 444-447.  
17310255 D.J.Seward, G.Cubberley, S.Kim, M.Schonewald, L.Zhang, B.Tripet, and D.L.Bentley (2007).
Demethylation of trimethylated histone H3 Lys4 in vivo by JARID1 JmjC proteins.
  Nat Struct Mol Biol, 14, 240-242.  
17525233 E.R.Lee, F.E.Murdoch, and M.K.Fritsch (2007).
High histone acetylation and decreased polycomb repressive complex 2 member levels regulate gene specific transcriptional changes during early embryonic stem cell differentiation induced by retinoic acid.
  Stem Cells, 25, 2191-2199.  
17713579 E.V.Benevolenskaya (2007).
Histone H3K4 demethylases are essential in development and differentiation.
  Biochem Cell Biol, 85, 435-443.  
17988933 G.Kustatscher, and A.G.Ladurner (2007).
Modular paths to 'decoding' and 'wiping' histone lysine methylation.
  Curr Opin Chem Biol, 11, 628-635.  
17245432 I.du Chéné, E.Basyuk, Y.L.Lin, R.Triboulet, A.Knezevich, C.Chable-Bessia, C.Mettling, V.Baillat, J.Reynes, P.Corbeau, E.Bertrand, A.Marcello, S.Emiliani, R.Kiernan, and M.Benkirane (2007).
Suv39H1 and HP1gamma are responsible for chromatin-mediated HIV-1 transcriptional silencing and post-integration latency.
  EMBO J, 26, 424-435.  
17589523 J.F.Couture, E.Collazo, P.A.Ortiz-Tello, J.S.Brunzelle, and R.C.Trievel (2007).
Specificity and mechanism of JMJD2A, a trimethyllysine-specific histone demethylase.
  Nat Struct Mol Biol, 14, 689-695.
PDB codes: 2q8c 2q8d 2q8e
17470555 J.Fang, G.J.Hogan, G.Liang, J.D.Lieb, and Y.Zhang (2007).
The Saccharomyces cerevisiae histone demethylase Jhd1 fine-tunes the distribution of H3K36me2.
  Mol Cell Biol, 27, 5055-5065.  
17676028 J.R.Wilson (2007).
Targeting the JMJD2A histone lysine demethylase.
  Nat Struct Mol Biol, 14, 682-684.  
17311883 J.Secombe, L.Li, L.Carlos, and R.N.Eisenman (2007).
The Trithorax group protein Lid is a trimethyl histone H3K4 demethylase required for dMyc-induced cell growth.
  Genes Dev, 21, 537-551.  
17135241 K.S.Hewitson, B.M.Liénard, M.A.McDonough, I.J.Clifton, D.Butler, A.S.Soares, N.J.Oldham, L.A.McNeill, and C.J.Schofield (2007).
Structural and mechanistic studies on the inhibition of the hypoxia-inducible transcription factor hydroxylases by tricarboxylic acid cycle intermediates.
  J Biol Chem, 282, 3293-3301.
PDB codes: 2cgn 2cgo
17363312 K.Yamane, K.Tateishi, R.J.Klose, J.Fang, L.A.Fabrizio, H.Erdjument-Bromage, J.Taylor-Papadimitriou, P.Tempst, and Y.Zhang (2007).
PLU-1 is an H3K4 demethylase involved in transcriptional repression and breast cancer cell proliferation.
  Mol Cell, 25, 801-812.  
17550896 M.Huarte, F.Lan, T.Kim, M.W.Vaughn, M.Zaratiegui, R.A.Martienssen, S.Buratowski, and Y.Shi (2007).
The fission yeast Jmj2 reverses histone H3 Lysine 4 trimethylation.
  J Biol Chem, 282, 21662-21670.  
17606868 M.Yuneva, N.Zamboni, P.Oefner, R.Sachidanandam, and Y.Lazebnik (2007).
Deficiency in glutamine but not glucose induces MYC-dependent apoptosis in human cells.
  J Cell Biol, 178, 93.  
17504018 P.Stavropoulos, and A.Hoelz (2007).
Lysine-specific demethylase 1 as a potential therapeutic target.
  Expert Opin Ther Targets, 11, 809-820.  
17897944 R.Anand, and R.Marmorstein (2007).
Structure and mechanism of lysine-specific demethylase enzymes.
  J Biol Chem, 282, 35425-35429.  
17371840 R.J.Klose, K.E.Gardner, G.Liang, H.Erdjument-Bromage, P.Tempst, and Y.Zhang (2007).
Demethylation of histone H3K36 and H3K9 by Rph1: a vestige of an H3K9 methylation system in Saccharomyces cerevisiae?
  Mol Cell Biol, 27, 3951-3961.  
17342184 R.J.Klose, and Y.Zhang (2007).
Regulation of histone methylation by demethylimination and demethylation.
  Nat Rev Mol Cell Biol, 8, 307-318.  
18003914 S.Hong, Y.W.Cho, L.R.Yu, H.Yu, T.D.Veenstra, and K.Ge (2007).
Identification of JmjC domain-containing UTX and JMJD3 as histone H3 lysine 27 demethylases.
  Proc Natl Acad Sci U S A, 104, 18439-18444.  
17984971 S.Lall (2007).
Primers on chromatin.
  Nat Struct Mol Biol, 14, 1110-1115.  
17589501 S.S.Ng, K.L.Kavanagh, M.A.McDonough, D.Butler, E.S.Pilka, B.M.Lienard, J.E.Bray, P.Savitsky, O.Gileadi, F.von Delft, N.R.Rose, J.Offer, J.C.Scheinost, T.Borowski, M.Sundstrom, C.J.Schofield, and U.Oppermann (2007).
Crystal structures of histone demethylase JMJD2A reveal basis for substrate specificity.
  Nature, 448, 87-91.
PDB codes: 2oq6 2oq7 2os2 2ot7 2ox0
17525156 T.Kim, and S.Buratowski (2007).
Two Saccharomyces cerevisiae JmjC domain proteins demethylate histone H3 Lys36 in transcribed regions to promote elongation.
  J Biol Chem, 282, 20827-20835.  
17320507 T.Kouzarides (2007).
Chromatin modifications and their function.
  Cell, 128, 693-705.  
17374386 X.Cheng, and X.Zhang (2007).
Structural dynamics of protein lysine methylation and demethylation.
  Mutat Res, 618, 102-115.  
17277881 X.Tian, and J.Fang (2007).
Current perspectives on histone demethylases.
  Acta Biochim Biophys Sin (Shanghai), 39, 81-88.  
17218267 Y.Shi, and J.R.Whetstine (2007).
Dynamic regulation of histone lysine methylation by demethylases.
  Mol Cell, 25, 1.  
17923864 Y.Xiang, Z.Zhu, G.Han, H.Lin, L.Xu, and C.D.Chen (2007).
JMJD3 is a histone H3K27 demethylase.
  Cell Res, 17, 850-857.  
18048344 Y.Xiang, Z.Zhu, G.Han, X.Ye, B.Xu, Z.Peng, Y.Ma, Y.Yu, H.Lin, A.P.Chen, and C.D.Chen (2007).
JARID1B is a histone H3 lysine 4 demethylase up-regulated in prostate cancer.
  Proc Natl Acad Sci U S A, 104, 19226-19231.  
17567753 Z.Chen, J.Zang, J.Kappler, X.Hong, F.Crawford, Q.Wang, F.Lan, C.Jiang, J.Whetstine, S.Dai, K.Hansen, Y.Shi, and G.Zhang (2007).
Structural basis of the recognition of a methylated histone tail by JMJD2A.
  Proc Natl Acad Sci U S A, 104, 10818-10823.
PDB codes: 2p5b 2pxj
17018288 A.G.Ladurner (2006).
Rheostat control of gene expression by metabolites.
  Mol Cell, 24, 1.  
16959570 C.J.Nelson, H.Santos-Rosa, and T.Kouzarides (2006).
Proline isomerization of histone H3 regulates lysine methylation and gene expression.
  Cell, 126, 905-916.  
17070031 J.F.Couture, and R.C.Trievel (2006).
Histone-modifying enzymes: encrypting an enigmatic epigenetic code.
  Curr Opin Struct Biol, 16, 753-760.  
16943429 M.D.Gearhart, C.M.Corcoran, J.A.Wamstad, and V.J.Bardwell (2006).
Polycomb group and SCF ubiquitin ligases are found in a novel BCOR complex that is recruited to BCL6 targets.
  Mol Cell Biol, 26, 6880-6889.  
16885027 M.Yang, C.B.Gocke, X.Luo, D.Borek, D.R.Tomchick, M.Machius, Z.Otwinowski, and H.Yu (2006).
Structural basis for CoREST-dependent demethylation of nucleosomes by the human LSD1 histone demethylase.
  Mol Cell, 23, 377-387.
PDB code: 2iw5
16983801 R.J.Klose, E.M.Kallin, and Y.Zhang (2006).
JmjC-domain-containing proteins and histone demethylation.
  Nat Rev Genet, 7, 715-727.  
16956976 Y.Chen, Y.Yang, F.Wang, K.Wan, K.Yamane, Y.Zhang, and M.Lei (2006).
Crystal structure of human histone lysine-specific demethylase 1 (LSD1).
  Proc Natl Acad Sci U S A, 103, 13956-13961.
PDB code: 2hko
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.

 

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