2mdi

From Proteopedia

(Difference between revisions)

Current revision

Solution structure of the PP2WW mutant (KPP2WW) of HYPB

Structural highlights

2mdi is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SETD2_HUMAN Histone methyltransferase that methylates 'Lys-36' of histone H3. H3 'Lys-36' methylation represents a specific tag for epigenetic transcriptional activation. Probably plays a role in chromatin structure modulation during elongation via its interaction with hyperphosphorylated POLR2A. Binds DNA at promoters. May also act as a transcription activator that binds to promoters. Binds to the promoters of adenovirus 12 E1A gene in case of infection, possibly leading to regulate its expression.^[1]

Publication Abstract from PubMed

Huntington's disease (HD) is an autosomally dominant neurodegenerative disorder caused by expansion of polyglutamine (polyQ) in the huntingtin (Htt) protein. Htt yeast two-hybrid protein B (HYPB/SETD2), a histone methyltransferase, directly interacts with Htt and is involved in HD pathology. Using NMR techniques, we characterized a polyproline (polyP) stretch at the C terminus of HYPB, which directly interacts with the following WW domain and leads this domain predominantly to be in a closed conformational state. The solution structure shows that the polyP stretch extends from the back and binds to the WW core domain in a typical binding mode. This autoinhibitory structure regulates interaction between the WW domain of HYPB and the proline-rich region (PRR) of Htt, as evidenced by NMR and immunofluorescence techniques. This work provides structural and mechanistic insights into the intramolecular regulation of the WW domain in Htt-interacting partners and will be helpful for understanding the pathology of HD.

Autoinhibitory structure of the WW domain of HYPB/SETD2 regulates its interaction with the proline-rich region of huntingtin.,Gao YG, Yang H, Zhao J, Jiang YJ, Hu HY Structure. 2014 Mar 4;22(3):378-86. doi: 10.1016/j.str.2013.12.005. Epub 2014 Jan, 9. PMID:24412394^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Sun XJ, Wei J, Wu XY, Hu M, Wang L, Wang HH, Zhang QH, Chen SJ, Huang QH, Chen Z. Identification and characterization of a novel human histone H3 lysine 36-specific methyltransferase. J Biol Chem. 2005 Oct 21;280(42):35261-71. Epub 2005 Aug 22. PMID:16118227 doi:http://dx.doi.org/M504012200
↑ Gao YG, Yang H, Zhao J, Jiang YJ, Hu HY. Autoinhibitory structure of the WW domain of HYPB/SETD2 regulates its interaction with the proline-rich region of huntingtin. Structure. 2014 Mar 4;22(3):378-86. doi: 10.1016/j.str.2013.12.005. Epub 2014 Jan, 9. PMID:24412394 doi:http://dx.doi.org/10.1016/j.str.2013.12.005

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2mdi"

Categories: Homo sapiens | Large Structures | Gao YG | Hu HY

@@ Line 4: / Line 4: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[2mdi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MDI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MDI FirstGlance]. <br>
-</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=2mdi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mdi OCA], [https://pdbe.org/2mdi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mdi RCSB], [https://www.ebi.ac.uk/pdbsum/2mdi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mdi ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2mdi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mdi OCA], [https://pdbe.org/2mdi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mdi RCSB], [https://www.ebi.ac.uk/pdbsum/2mdi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mdi ProSAT]</span></td></tr>
 </table>
 == Function ==

2mdi

From Proteopedia

Current revision

Solution structure of the PP2WW mutant (KPP2WW) of HYPB

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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