Retinoblastoma-binding protein

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<StructureSection load='' size='350' side='right' scene='48/485630/Cv/1' caption='Human retinoblastoma-binding protein 7 (green) complex with histone H4 helix (magenta) and As ion (purple) [[3cfs]]'>
<StructureSection load='' size='350' side='right' scene='48/485630/Cv/1' caption='Human retinoblastoma-binding protein 7 (green) complex with histone H4 helix (magenta) and As ion (purple) [[3cfs]]'>
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__TOC__
== Function ==
== Function ==
'''Retinoblastoma-binding protein''' (RBBP) or '''histone-binding protein''' are nuclear proteins implicated in the regulation of transcription and differentiation by the retinoblastoma tumor suppressor protein<ref>PMID:9697699</ref>.<br />
'''Retinoblastoma-binding protein''' (RBBP) or '''histone-binding protein''' are nuclear proteins implicated in the regulation of transcription and differentiation by the retinoblastoma tumor suppressor protein<ref>PMID:9697699</ref>.<br />
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* '''RBBP2''' demethylates histone H3 at lysine 4.<br />
* '''RBBP2''' demethylates histone H3 at lysine 4.<br />
* '''RBBP2 homolog''' see KDM5B in [[Lysine-specific histone demethylase]].<br />
* '''RBBP2 homolog''' see KDM5B in [[Lysine-specific histone demethylase]].<br />
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* '''RBBP5''' is involved in methylation and dimethylation of histone H3.<br />
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* '''RBBP5''' is involved in methylation and dimethylation of histone H3<ref>PMID:31544921</ref>.<br />
* '''RBBP6''' promotes p53 degradation<ref>PMID:21676486</ref>.<br />
* '''RBBP6''' promotes p53 degradation<ref>PMID:21676486</ref>.<br />
* '''RBBP7''' is a WD-repeat protein that interacts with histone deacetylases<ref>PMID:12376095</ref>.<br />
* '''RBBP7''' is a WD-repeat protein that interacts with histone deacetylases<ref>PMID:12376095</ref>.<br />
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== Structural highlights ==
== Structural highlights ==
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<scene name='48/485630/Cv/4'>RBBP7 interacts with histone H4 in a pocket between its N-terminal α helix</scene> and its negatively charged <scene name='48/485630/Cv/5'>PP loop which contains 2 consecutive Pro residues</scene><ref>PMID:18571423</ref>.<br />.
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<scene name='48/485630/Cv/6'>RBBP7 interacts with histone H4 in a pocket between its N-terminal α helix</scene> and its negatively charged <scene name='48/485630/Cv/7'>PP loop which contains 2 consecutive Pro residues</scene><ref>PMID:18571423</ref>.<br />.
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</StructureSection>
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==3D structures of retinoblastoma-binding protein==
==3D structures of retinoblastoma-binding protein==
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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[[Retinoblastoma-binding protein 3D structures]]
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{{#tree:id=OrganizedByTopic|openlevels=0|
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*Retinoblastoma-binding protein 1
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</StructureSection>
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**[[2yrv]], [[2lcc]] – hRBBP1 AT-rich interactive domain – human – NMR<BR />
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**[[2mam]] - hRBBP1 double tudor domain - NMR<br />
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*Retinoblastoma-binding protein 2
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**[[2jxj]] – hRBBP2 ARID domain + histone H3 – NMR<BR />
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**[[2kgg]] – hRBBP2 C terminal PHD zinc finger – NMR<BR />
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**[[2kgi]] - hRBBP2 C terminal PHD zinc finger + histone H3 – NMR<BR />
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**[[3gl6]] - hRBBP2 C terminal PHD zinc finger + histone H3 N terminal
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*Retinoblastoma-binding protein 4 or histone-binding protein RBBP4
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**[[3gfc]] – hRBBP4<br />
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**[[2xu7]] – hRBBP4 + zinc finger protein ZFPM1 RBBP4-binding domain<br />
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**[[4pby]], [[4pbz]], [[4pc0]] – hRBBP4 + metastasis-associated protein<br />
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**[[4r7a]] – hRBBP4 + PHD protein 6 peptide<br />
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**[[6bw4]] – hRBBP4 + Prdm16 peptide<br />
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**[[6bw3]] – hRBBP4 + Mds1 peptide<br />
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**[[5y1u]] – hRBBP4 + Aebp2 peptide<br />
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**[[5xxq]] – hRBBP4 + Znf827 peptide<br />
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**[[5wak]] – hRBBP4 + Suz12 peptide<br />
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**[[5vtb]] – hRBBP4 + Bcl11A peptide<br />
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**[[5xwr]] – hRBBP4 + peptide<br />
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**[[5fxy]], [[6g16]] – hRBBP4 + MTA1 protein <br />
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**[[5wai]] – hRBBP4 + Suz12 + Jumonji + Aebp2 <br />
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**[[6c23]] – hRBBP4 + Suz12 + Jumonji + Ezh2 + Eed + Jarid2 + Aebp2 – Cryo EM <br />
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*Retinoblastoma-binding protein 6
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**[[2c7h]] – hRBBP6 DWNN domain – NMR<BR />
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**[[2ysa]] - hRBBP6 zinc finger CCHC domain – NMR<BR />
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**[[2yur]], [[3ztg]] - hRBBP6 ring finger domain – NMR<BR />
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*Retinoblastoma-binding protein 7
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**[[3cfs]], [[3cfv]] – hRBBP7 + histone H4 helix
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*Retinoblastoma-binding protein 8
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**[[4d2h]] – hRBBP8<br />
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*Retinoblastoma-binding protein 9
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**[[2qs9]] – hRBBP9
 
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}}
 
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

Human retinoblastoma-binding protein 7 (green) complex with histone H4 helix (magenta) and As ion (purple) 3cfs

Drag the structure with the mouse to rotate

References

  1. ↑ Woitach JT, Zhang M, Niu CH, Thorgeirsson SS. A retinoblastoma-binding protein that affects cell-cycle control and confers transforming ability. Nat Genet. 1998 Aug;19(4):371-4. PMID:9697699 doi:http://dx.doi.org/10.1038/1258
  2. ↑ Fattaey AR, Helin K, Dembski MS, Dyson N, Harlow E, Vuocolo GA, Hanobik MG, Haskell KM, Oliff A, Defeo-Jones D, et al.. Characterization of the retinoblastoma binding proteins RBP1 and RBP2. Oncogene. 1993 Nov;8(11):3149-56. PMID:8414517
  3. ↑ Han J, Li T, Li Y, Li M, Wang X, Peng C, Su C, Li N, Li Y, Xu Y, Chen Y. The internal interaction in RBBP5 regulates assembly and activity of MLL1 methyltransferase complex. Nucleic Acids Res. 2019 Sep 23. pii: 5572575. doi: 10.1093/nar/gkz819. PMID:31544921 doi:http://dx.doi.org/10.1093/nar/gkz819
  4. ↑ Motadi LR, Bhoola KD, Dlamini Z. Expression and function of retinoblastoma binding protein 6 (RBBP6) in human lung cancer. Immunobiology. 2011 Oct;216(10):1065-73. doi: 10.1016/j.imbio.2011.05.004. Epub, 2011 May 17. PMID:21676486 doi:http://dx.doi.org/10.1016/j.imbio.2011.05.004
  5. ↑ Yang J, Kiefer S, Rauchman M. Characterization of the gene encoding mouse retinoblastoma binding protein-7, a component of chromatin-remodeling complexes. Genomics. 2002 Oct;80(4):407-15. PMID:12376095
  6. ↑ Vorobiev SM, Huang YJ, Seetharaman J, Xiao R, Acton TB, Montelione GT, Tong L. Human retinoblastoma binding protein 9, a serine hydrolase implicated in pancreatic cancers. Protein Pept Lett. 2012 Feb;19(2):194-7. PMID:21933118
  7. ↑ Murzina NV, Pei XY, Zhang W, Sparkes M, Vicente-Garcia J, Pratap JV, McLaughlin SH, Ben-Shahar TR, Verreault A, Luisi BF, Laue ED. Structural basis for the recognition of histone H4 by the histone-chaperone RbAp46. Structure. 2008 Jul;16(7):1077-85. Epub 2008 Jun 19. PMID:18571423 doi:http://dx.doi.org/10.1016/j.str.2008.05.006

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