6odb: Difference between revisions

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'''Unreleased structure'''


The entry 6odb is ON HOLD
==Crystal structure of HDAC8 in complex with compound 3==
<StructureSection load='6odb' size='340' side='right'caption='[[6odb]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6odb]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ODB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ODB FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=M8G:N-{2-[(1E)-3-(hydroxyamino)-3-oxoprop-1-en-1-yl]phenyl}-2-phenoxybenzamide'>M8G</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6odb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6odb OCA], [https://pdbe.org/6odb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6odb RCSB], [https://www.ebi.ac.uk/pdbsum/6odb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6odb ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HDAC8_HUMAN HDAC8_HUMAN] Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. May play a role in smooth muscle cell contractility.<ref>PMID:10748112</ref> <ref>PMID:10926844</ref> <ref>PMID:10922473</ref> <ref>PMID:14701748</ref>


Authors: Zheng, X., Conti, C., Caravella, J., Zablocki, M.-M., Bair, K., Barczak, N., Han, B., Lancia Jr., D., Liu, C., Martin, M., Ng, P.Y., Rudnitskaya, A., Thomason, J.J., Garcia-Dancey, R., Hardy, C., Lahdenranta, J., Leng, C., Li, P., Pardo, E., Saldahna, A., Tan, T., Toms, A.V., Yao, L., Zhang, C.
==See Also==
 
*[[Histone deacetylase 3D structures|Histone deacetylase 3D structures]]
Description: Crystal structure of HDAC8 in complex with compound 3
== References ==
[[Category: Unreleased Structures]]
<references/>
[[Category: Tan, T]]
__TOC__
[[Category: Rudnitskaya, A]]
</StructureSection>
[[Category: Leng, C]]
[[Category: Homo sapiens]]
[[Category: Barczak, N]]
[[Category: Large Structures]]
[[Category: Lancia Jr]]
[[Category: Bair K]]
[[Category: Han, B]]
[[Category: Barczak N]]
[[Category: Zablocki, M.-M]]
[[Category: Caravella J]]
[[Category: Yao, L]]
[[Category: Conti C]]
[[Category: Martin, M]]
[[Category: Garcia-Dancey R]]
[[Category: Bair, K]]
[[Category: Han B]]
[[Category: Toms, A.V]]
[[Category: Hardy C]]
[[Category: Pardo, E]]
[[Category: Lahdenranta J]]
[[Category: Zheng, X]]
[[Category: Lancia Jr D]]
[[Category: Liu, C]]
[[Category: Leng C]]
[[Category: Conti, C]]
[[Category: Li P]]
[[Category: Hardy, C]]
[[Category: Liu C]]
[[Category: Lahdenranta, J]]
[[Category: Martin M]]
[[Category: Caravella, J]]
[[Category: Ng PY]]
[[Category: Saldahna, A]]
[[Category: Pardo E]]
[[Category: Garcia-Dancey, R]]
[[Category: Rudnitskaya A]]
[[Category: Zhang, C]]
[[Category: Saldahna A]]
[[Category: D]]
[[Category: Tan T]]
[[Category: Li, P]]
[[Category: Thomason JJ]]
[[Category: Ng, P.Y]]
[[Category: Toms AV]]
[[Category: Thomason, J.J]]
[[Category: Yao L]]
[[Category: Zablocki M-M]]
[[Category: Zhang C]]
[[Category: Zheng X]]

Latest revision as of 10:08, 11 October 2023

Crystal structure of HDAC8 in complex with compound 3Crystal structure of HDAC8 in complex with compound 3

Structural highlights

6odb is a 3 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.7Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HDAC8_HUMAN Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. May play a role in smooth muscle cell contractility.[1] [2] [3] [4]

See Also

References

  1. ↑ Hu E, Chen Z, Fredrickson T, Zhu Y, Kirkpatrick R, Zhang GF, Johanson K, Sung CM, Liu R, Winkler J. Cloning and characterization of a novel human class I histone deacetylase that functions as a transcription repressor. J Biol Chem. 2000 May 19;275(20):15254-64. PMID:10748112 doi:http://dx.doi.org/10.1074/jbc.M908988199
  2. ↑ Buggy JJ, Sideris ML, Mak P, Lorimer DD, McIntosh B, Clark JM. Cloning and characterization of a novel human histone deacetylase, HDAC8. Biochem J. 2000 Aug 15;350 Pt 1:199-205. PMID:10926844
  3. ↑ Van den Wyngaert I, de Vries W, Kremer A, Neefs J, Verhasselt P, Luyten WH, Kass SU. Cloning and characterization of human histone deacetylase 8. FEBS Lett. 2000 Jul 28;478(1-2):77-83. PMID:10922473
  4. ↑ Lee H, Rezai-Zadeh N, Seto E. Negative regulation of histone deacetylase 8 activity by cyclic AMP-dependent protein kinase A. Mol Cell Biol. 2004 Jan;24(2):765-73. PMID:14701748

6odb, resolution 2.70Å

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