2brf

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==CRYSTAL STRUCTURE OF THE FHA DOMAIN OF HUMAN POLYNUCLEOTIDE KINASE 3' PHOSPHATASE==
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<StructureSection load='2brf' size='340' side='right' caption='[[2brf]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
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==Crystal Structure of the FHA Domain of Human Polynucleotide Kinase 3' Phosphatase==
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<StructureSection load='2brf' size='340' side='right'caption='[[2brf]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2brf]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BRF FirstGlance]. <br>
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<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>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>
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</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>
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<tr><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://www.rcsb.org/pdb/explore.do?structureId=2brf RCSB], [http://www.ebi.ac.uk/pdbsum/2brf PDBsum]</span></td></tr>
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<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>
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<table>
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<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>
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</table>
== Disease ==
== Disease ==
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[[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>
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[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 ==
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[[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>
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[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]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/br/2brf_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/br/2brf_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2brf ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 2brf" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Ali, A A.E.]]
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[[Category: Large Structures]]
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[[Category: Oliver, A W.]]
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[[Category: Ali AAE]]
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[[Category: Pearl, L H.]]
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[[Category: Oliver AW]]
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[[Category: Ber]]
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[[Category: Pearl LH]]
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[[Category: Bifunctional]]
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[[Category: Dna repair]]
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[[Category: Dsbr]]
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[[Category: Fha]]
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[[Category: Forkhead-associated]]
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[[Category: Hydrolase-transferase complex]]
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[[Category: Hydrolase/transferase]]
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[[Category: Pnk]]
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[[Category: Pnkp]]
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[[Category: Polynucleotide kinase 3' phosphatase]]
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[[Category: Ssbr]]
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[[Category: Transferase]]
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[[Category: Xrcc1]]
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[[Category: Xrcc4 hydrolase]]
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Current revision

Crystal Structure of the FHA Domain of Human Polynucleotide Kinase 3' Phosphatase

PDB ID 2brf

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