7ynx: Difference between revisions

Revision as of 17:00, 26 April 2023

Crystal structure of Pirh2 bound to poly-Ala peptide

Structural highlights

7ynx is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	NA, SO4, ZN
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ZN363_HUMAN Mediates E3-dependent ubiquitination and proteasomal degradation of target proteins, including p53/TP53, P73, HDAC1 and CDKN1B. Preferentially acts on tetrameric p53/TP53. Monoubiquitinates the translesion DNA polymerase POLH. Contributes to the regulation of the cell cycle progression. Increases AR transcription factor activity.^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7]

References

↑ Corcoran CA, Montalbano J, Sun H, He Q, Huang Y, Sheikh MS. Identification and characterization of two novel isoforms of Pirh2 ubiquitin ligase that negatively regulate p53 independent of RING finger domains. J Biol Chem. 2009 Aug 14;284(33):21955-70. Epub 2009 May 29. PMID:19483087 doi:https://dx.doi.org/M109.024232
↑ Logan IR, Gaughan L, McCracken SR, Sapountzi V, Leung HY, Robson CN. Human PIRH2 enhances androgen receptor signaling through inhibition of histone deacetylase 1 and is overexpressed in prostate cancer. Mol Cell Biol. 2006 Sep;26(17):6502-10. PMID:16914734 doi:https://dx.doi.org/10.1128/MCB.00147-06
↑ Hattori T, Isobe T, Abe K, Kikuchi H, Kitagawa K, Oda T, Uchida C, Kitagawa M. Pirh2 promotes ubiquitin-dependent degradation of the cyclin-dependent kinase inhibitor p27Kip1. Cancer Res. 2007 Nov 15;67(22):10789-95. PMID:18006823 doi:https://dx.doi.org/10.1158/0008-5472.CAN-07-2033
↑ Maruyama S, Miyajima N, Bohgaki M, Tsukiyama T, Shigemura M, Nonomura K, Hatakeyama S. Ubiquitylation of epsilon-COP by PIRH2 and regulation of the secretion of PSA. Mol Cell Biochem. 2008 Jan;307(1-2):73-82. Epub 2007 Aug 25. PMID:17721809 doi:https://dx.doi.org/10.1007/s11010-007-9586-3
↑ Wu H, Zeinab RA, Flores ER, Leng RP. Pirh2, a ubiquitin E3 ligase, inhibits p73 transcriptional activity by promoting its ubiquitination. Mol Cancer Res. 2011 Dec;9(12):1780-90. doi: 10.1158/1541-7786.MCR-11-0157. Epub , 2011 Oct 12. PMID:21994467 doi:https://dx.doi.org/10.1158/1541-7786.MCR-11-0157
↑ Jung YS, Hakem A, Hakem R, Chen X. Pirh2 E3 ubiquitin ligase monoubiquitinates DNA polymerase eta to suppress translesion DNA synthesis. Mol Cell Biol. 2011 Oct;31(19):3997-4006. doi: 10.1128/MCB.05808-11. Epub 2011, Jul 26. PMID:21791603 doi:https://dx.doi.org/10.1128/MCB.05808-11
↑ Sheng Y, Laister RC, Lemak A, Wu B, Tai E, Duan S, Lukin J, Sunnerhagen M, Srisailam S, Karra M, Benchimol S, Arrowsmith CH. Molecular basis of Pirh2-mediated p53 ubiquitylation. Nat Struct Mol Biol. 2008 Dec;15(12):1334-42. Epub 2008 Nov 30. PMID:19043414 doi:https://dx.doi.org/10.1038/nsmb.1521

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OCA

[1] Corcoran CA, Montalbano J, Sun H, He Q, Huang Y, Sheikh MS. Identification and characterization of two novel isoforms of Pirh2 ubiquitin ligase that negatively regulate p53 independent of RING finger domains. J Biol Chem. 2009 Aug 14;284(33):21955-70. Epub 2009 May 29. PMID:19483087 doi:https://dx.doi.org/M109.024232

[2] Logan IR, Gaughan L, McCracken SR, Sapountzi V, Leung HY, Robson CN. Human PIRH2 enhances androgen receptor signaling through inhibition of histone deacetylase 1 and is overexpressed in prostate cancer. Mol Cell Biol. 2006 Sep;26(17):6502-10. PMID:16914734 doi:https://dx.doi.org/10.1128/MCB.00147-06

[3] Hattori T, Isobe T, Abe K, Kikuchi H, Kitagawa K, Oda T, Uchida C, Kitagawa M. Pirh2 promotes ubiquitin-dependent degradation of the cyclin-dependent kinase inhibitor p27Kip1. Cancer Res. 2007 Nov 15;67(22):10789-95. PMID:18006823 doi:https://dx.doi.org/10.1158/0008-5472.CAN-07-2033

[4] Maruyama S, Miyajima N, Bohgaki M, Tsukiyama T, Shigemura M, Nonomura K, Hatakeyama S. Ubiquitylation of epsilon-COP by PIRH2 and regulation of the secretion of PSA. Mol Cell Biochem. 2008 Jan;307(1-2):73-82. Epub 2007 Aug 25. PMID:17721809 doi:https://dx.doi.org/10.1007/s11010-007-9586-3

[5] Wu H, Zeinab RA, Flores ER, Leng RP. Pirh2, a ubiquitin E3 ligase, inhibits p73 transcriptional activity by promoting its ubiquitination. Mol Cancer Res. 2011 Dec;9(12):1780-90. doi: 10.1158/1541-7786.MCR-11-0157. Epub , 2011 Oct 12. PMID:21994467 doi:https://dx.doi.org/10.1158/1541-7786.MCR-11-0157

[6] Jung YS, Hakem A, Hakem R, Chen X. Pirh2 E3 ubiquitin ligase monoubiquitinates DNA polymerase eta to suppress translesion DNA synthesis. Mol Cell Biol. 2011 Oct;31(19):3997-4006. doi: 10.1128/MCB.05808-11. Epub 2011, Jul 26. PMID:21791603 doi:https://dx.doi.org/10.1128/MCB.05808-11

[7] Sheng Y, Laister RC, Lemak A, Wu B, Tai E, Duan S, Lukin J, Sunnerhagen M, Srisailam S, Karra M, Benchimol S, Arrowsmith CH. Molecular basis of Pirh2-mediated p53 ubiquitylation. Nat Struct Mol Biol. 2008 Dec;15(12):1334-42. Epub 2008 Nov 30. PMID:19043414 doi:https://dx.doi.org/10.1038/nsmb.1521

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 7ynx is ON HOLD  until Paper Publication
+==Crystal structure of Pirh2 bound to poly-Ala peptide==
+<StructureSection load='7ynx' size='340' side='right'caption='[[7ynx]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
-Authors:
+== Structural highlights ==
+<table><tr><td colspan='2'>[[7ynx]] is a 2 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=7YNX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7YNX FirstGlance]. <br>
-Description:
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-[[Category: Unreleased Structures]]
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7ynx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ynx OCA], [https://pdbe.org/7ynx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ynx RCSB], [https://www.ebi.ac.uk/pdbsum/7ynx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ynx ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/ZN363_HUMAN ZN363_HUMAN] Mediates E3-dependent ubiquitination and proteasomal degradation of target proteins, including p53/TP53, P73, HDAC1 and CDKN1B. Preferentially acts on tetrameric p53/TP53. Monoubiquitinates the translesion DNA polymerase POLH. Contributes to the regulation of the cell cycle progression. Increases AR transcription factor activity.<ref>PMID:19483087</ref> <ref>PMID:16914734</ref> <ref>PMID:18006823</ref> <ref>PMID:17721809</ref> <ref>PMID:21994467</ref> <ref>PMID:21791603</ref> <ref>PMID:19043414</ref>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Dong C]]
+[[Category: Li Y]]
+[[Category: Yan X]]

7ynx: Difference between revisions

Revision as of 17:00, 26 April 2023

Crystal structure of Pirh2 bound to poly-Ala peptide

Structural highlights

Function

References

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