6ej1: Difference between revisions

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'''Unreleased structure'''


The entry 6ej1 is ON HOLD
==Crystal structure of KDM5B in complex with KDOPZ48a.==
<StructureSection load='6ej1' size='340' side='right'caption='[[6ej1]], [[Resolution|resolution]] 2.07&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6ej1]] is a 1 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=6EJ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6EJ1 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]] 2.07&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B7Q:5-[1-[1-(2-chloranylethanoyl)piperidin-4-yl]pyrazol-4-yl]-7-oxidanylidene-6-propan-2-yl-4~{H}-pyrazolo[1,5-a]pyrimidine-3-carbonitrile'>B7Q</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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=6ej1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ej1 OCA], [https://pdbe.org/6ej1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ej1 RCSB], [https://www.ebi.ac.uk/pdbsum/6ej1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ej1 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/KDM5B_HUMAN KDM5B_HUMAN] Histone demethylase that demethylates 'Lys-4' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-9' or H3 'Lys-27'. Demethylates trimethylated, dimethylated and monomethylated H3 'Lys-4'. Acts as a transcriptional corepressor for FOXG1B and PAX9. Favors the proliferation of breast cancer cells by repressing tumor suppressor genes such as BRCA1 and HOXA5. In contrast, may act as a tumor suppressor for melanoma.<ref>PMID:12657635</ref> <ref>PMID:16645588</ref> <ref>PMID:17320161</ref> <ref>PMID:17363312</ref>


Authors: Srikannathasan, v., Szykowska, A., Newman, J.A., Kupinska, K., Strain-Damerell, C., Burgess-Brown, N.A., Arrowsmith, C.H., Edwards, A., Bountra, C., Oppermann, U., Huber, K., von Delft, F.
==See Also==
 
*[[Lysine-specific histone demethylase 3D structures|Lysine-specific histone demethylase 3D structures]]
Description: Crystal structure of KDM5B in complex with KDOPZ48a.
*[[Retinoblastoma-binding protein 3D structures|Retinoblastoma-binding protein 3D structures]]
[[Category: Unreleased Structures]]
== References ==
[[Category: Burgess-Brown, N.A]]
<references/>
[[Category: Bountra, C]]
__TOC__
[[Category: Kupinska, K]]
</StructureSection>
[[Category: Huber, K]]
[[Category: Homo sapiens]]
[[Category: Arrowsmith, C.H]]
[[Category: Large Structures]]
[[Category: Oppermann, U]]
[[Category: Arrowsmith CH]]
[[Category: Szykowska, A]]
[[Category: Bountra C]]
[[Category: Von Delft, F]]
[[Category: Burgess-Brown NA]]
[[Category: Newman, J.A]]
[[Category: Edwards A]]
[[Category: Edwards, A]]
[[Category: Huber K]]
[[Category: Strain-Damerell, C]]
[[Category: Kupinska K]]
[[Category: Srikannathasan, V]]
[[Category: Newman JA]]
[[Category: Oppermann U]]
[[Category: Ruda GF]]
[[Category: Srikannathasan V]]
[[Category: Strain-Damerell C]]
[[Category: Szykowska A]]
[[Category: Vazquez-Rodriguez SA]]
[[Category: Wright M]]
[[Category: Von Delft F]]

Latest revision as of 15:35, 6 November 2024

Crystal structure of KDM5B in complex with KDOPZ48a.Crystal structure of KDM5B in complex with KDOPZ48a.

Structural highlights

6ej1 is a 1 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 2.07Å
Ligands:, , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

KDM5B_HUMAN Histone demethylase that demethylates 'Lys-4' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-9' or H3 'Lys-27'. Demethylates trimethylated, dimethylated and monomethylated H3 'Lys-4'. Acts as a transcriptional corepressor for FOXG1B and PAX9. Favors the proliferation of breast cancer cells by repressing tumor suppressor genes such as BRCA1 and HOXA5. In contrast, may act as a tumor suppressor for melanoma.[1] [2] [3] [4]

See Also

References

  1. ↑ Tan K, Shaw AL, Madsen B, Jensen K, Taylor-Papadimitriou J, Freemont PS. Human PLU-1 Has transcriptional repression properties and interacts with the developmental transcription factors BF-1 and PAX9. J Biol Chem. 2003 Jun 6;278(23):20507-13. Epub 2003 Mar 25. PMID:12657635 doi:http://dx.doi.org/10.1074/jbc.M301994200
  2. ↑ Roesch A, Becker B, Schneider-Brachert W, Hagen I, Landthaler M, Vogt T. Re-expression of the retinoblastoma-binding protein 2-homolog 1 reveals tumor-suppressive functions in highly metastatic melanoma cells. J Invest Dermatol. 2006 Aug;126(8):1850-9. Epub 2006 Apr 27. PMID:16645588 doi:http://dx.doi.org/10.1038/sj.jid.5700324
  3. ↑ Christensen J, Agger K, Cloos PA, Pasini D, Rose S, Sennels L, Rappsilber J, Hansen KH, Salcini AE, Helin K. RBP2 belongs to a family of demethylases, specific for tri-and dimethylated lysine 4 on histone 3. Cell. 2007 Mar 23;128(6):1063-76. Epub 2007 Feb 22. PMID:17320161 doi:S0092-8674(07)00182-1
  4. ↑ Yamane K, Tateishi K, Klose RJ, Fang J, Fabrizio LA, Erdjument-Bromage H, Taylor-Papadimitriou J, Tempst P, Zhang Y. PLU-1 is an H3K4 demethylase involved in transcriptional repression and breast cancer cell proliferation. Mol Cell. 2007 Mar 23;25(6):801-12. Epub 2007 Mar 15. PMID:17363312 doi:http://dx.doi.org/S1097-2765(07)00146-3

6ej1, resolution 2.07Å

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