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==Human poly(ADP-ribose) polymerase 3, catalytic fragment in complex with an inhibitor DR2313== | ==Human poly(ADP-ribose) polymerase 3, catalytic fragment in complex with an inhibitor DR2313== | ||
<StructureSection load='3c4h' size='340' side='right' caption='[[3c4h]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='3c4h' size='340' side='right'caption='[[3c4h]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3c4h]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3c4h]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C4H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3C4H FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=DRL:2-METHYL-3,5,7,8-TETRAHYDRO-4H-THIOPYRANO[4,3-D]PYRIMIDIN-4-ONE'>DRL</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=DRL:2-METHYL-3,5,7,8-TETRAHYDRO-4H-THIOPYRANO[4,3-D]PYRIMIDIN-4-ONE'>DRL</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2pa9|2pa9]], [[3c49|3c49]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2pa9|2pa9]], [[3c49|3c49]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PARP3, ADPRT3, ADPRTL3 ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PARP3, ADPRT3, ADPRTL3 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/NAD(+)_ADP-ribosyltransferase NAD(+) ADP-ribosyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.30 2.4.2.30] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3c4h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c4h OCA], [https://pdbe.org/3c4h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3c4h RCSB], [https://www.ebi.ac.uk/pdbsum/3c4h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3c4h ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/PARP3_HUMAN PARP3_HUMAN]] Involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. This modification follows DNA damages and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks. May link the DNA damage surveillance network to the mitotic fidelity checkpoint. Negatively influences the G1/S cell cycle progression without interfering with centrosome duplication. Binds DNA. May be involved in the regulation of PRC2 and PRC3 complex-dependent gene silencing.<ref>PMID:16924674</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 33: | Line 33: | ||
==See Also== | ==See Also== | ||
*[[Poly (ADP-ribose) polymerase|Poly (ADP-ribose) polymerase]] | *[[Poly(ADP-ribose) polymerase 3D structures|Poly(ADP-ribose) polymerase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 39: | Line 39: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
[[Category: Large Structures]] | |||
[[Category: Arrowsmith, C H]] | [[Category: Arrowsmith, C H]] | ||
[[Category: Berg, S Van den]] | [[Category: Berg, S Van den]] | ||
Revision as of 10:42, 27 January 2022
Human poly(ADP-ribose) polymerase 3, catalytic fragment in complex with an inhibitor DR2313Human poly(ADP-ribose) polymerase 3, catalytic fragment in complex with an inhibitor DR2313
Structural highlights
Function[PARP3_HUMAN] Involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. This modification follows DNA damages and appears as an obligatory step in a detection/signaling pathway leading to the reparation of DNA strand breaks. May link the DNA damage surveillance network to the mitotic fidelity checkpoint. Negatively influences the G1/S cell cycle progression without interfering with centrosome duplication. Binds DNA. May be involved in the regulation of PRC2 and PRC3 complex-dependent gene silencing.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedPoly(ADP-ribose) polymerases (PARPs) activate DNA repair mechanisms upon stress- and cytotoxin-induced DNA damage, and inhibition of PARP activity is a lead in cancer drug therapy. We present a structural and functional analysis of the PARP domain of human PARP-3 in complex with several inhibitors. Of these, KU0058948 is the strongest inhibitor of PARP-3 activity. The presented crystal structures highlight key features for potent inhibitor binding and suggest routes for creating isoenzyme-specific PARP inhibitors. Structural basis for inhibitor specificity in human poly(ADP-ribose) polymerase-3.,Lehtio L, Jemth AS, Collins R, Loseva O, Johansson A, Markova N, Hammarstrom M, Flores A, Holmberg-Schiavone L, Weigelt J, Helleday T, Schuler H, Karlberg T J Med Chem. 2009 May 14;52(9):3108-11. PMID:19354255[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCACategories:
- Human
- Large Structures
- Arrowsmith, C H
- Berg, S Van den
- Berglund, H
- Bountra, C
- Busam, R
- Collins, R
- Dahlgren, L G
- Edwards, A M
- Flodin, S
- Flores, A
- Graslund, S
- Hammarstrom, M
- Herman, M D
- Johansson, A
- Johansson, I
- Kallas, A
- Karlberg, T
- Kotenyova, T
- Lehtio, L
- Moche, M
- Nilsson, M E
- Nordlund, P
- Nyman, T
- Persson, C
- Structural genomic
- Sagemark, J
- Svensson, L
- Thorsell, A G
- Tresaugues, L
- Weigelt, J
- Welin, M
- Catalytic fragment
- Enzyme-inhibitor complex
- Glycosyltransferase
- Nad
- Nucleus
- Sgc
- Transferase