2brf: Difference between revisions

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<StructureSection load='2brf' size='340' side='right'caption='[[2brf]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
<StructureSection load='2brf' size='340' side='right'caption='[[2brf]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2brf]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BRF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BRF FirstGlance]. <br>
<table><tr><td colspan='2'>[[2brf]] 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=2BRF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BRF FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2brf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2brf OCA], [http://pdbe.org/2brf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2brf RCSB], [http://www.ebi.ac.uk/pdbsum/2brf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2brf ProSAT]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=2brf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2brf OCA], [https://pdbe.org/2brf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2brf RCSB], [https://www.ebi.ac.uk/pdbsum/2brf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2brf ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
[[http://www.uniprot.org/uniprot/PNKP_HUMAN PNKP_HUMAN]] Defects in PNKP are the cause of epileptic encephalopathy, early infantile, type 10 (EIEE10) [MIM:[http://omim.org/entry/613402 613402]]. A disease characterized by microcephaly, infantile-onset seizures, severe intellectual disability and delayed motor milestones with absent speech or only achieving a few words. Most patients also have behavioral problems with hyperactivity. Microcephaly is progressive and without neuronal migration or structural abnormalities, consistent with primary microcephaly.<ref>PMID:20118933</ref>
[https://www.uniprot.org/uniprot/PNKP_HUMAN PNKP_HUMAN] Defects in PNKP are the cause of epileptic encephalopathy, early infantile, type 10 (EIEE10) [MIM:[https://omim.org/entry/613402 613402]. A disease characterized by microcephaly, infantile-onset seizures, severe intellectual disability and delayed motor milestones with absent speech or only achieving a few words. Most patients also have behavioral problems with hyperactivity. Microcephaly is progressive and without neuronal migration or structural abnormalities, consistent with primary microcephaly.<ref>PMID:20118933</ref>  
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/PNKP_HUMAN PNKP_HUMAN]] Plays a key role in the repair of DNA damage, functioning as part of both the non-homologous end-joining (NHEJ) and base excision repair (BER) pathways. Through its two catalytic activities, PNK ensures that DNA termini are compatible with extension and ligation by either removing 3'-phosphates from, or by phosphorylating 5'-hydroxyl groups on, the ribose sugar of the DNA backbone.<ref>PMID:10446192</ref>
[https://www.uniprot.org/uniprot/PNKP_HUMAN PNKP_HUMAN] Plays a key role in the repair of DNA damage, functioning as part of both the non-homologous end-joining (NHEJ) and base excision repair (BER) pathways. Through its two catalytic activities, PNK ensures that DNA termini are compatible with extension and ligation by either removing 3'-phosphates from, or by phosphorylating 5'-hydroxyl groups on, the ribose sugar of the DNA backbone.<ref>PMID:10446192</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Ali, A A.E]]
[[Category: Ali AAE]]
[[Category: Oliver, A W]]
[[Category: Oliver AW]]
[[Category: Pearl, L H]]
[[Category: Pearl LH]]
[[Category: Ber]]
[[Category: Bifunctional]]
[[Category: Dna repair]]
[[Category: Dsbr]]
[[Category: Fha]]
[[Category: Forkhead-associated]]
[[Category: Hydrolase-transferase complex]]
[[Category: Hydrolase/transferase]]
[[Category: Pnk]]
[[Category: Pnkp]]
[[Category: Polynucleotide kinase 3' phosphatase]]
[[Category: Ssbr]]
[[Category: Transferase]]
[[Category: Xrcc1]]
[[Category: Xrcc4 hydrolase]]