8f5q

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'''Unreleased structure'''
 
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The entry 8f5q is ON HOLD until Paper Publication
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==Crystal structure of human PCNA in complex with the PIP box of FBH1==
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<StructureSection load='8f5q' size='340' side='right'caption='[[8f5q]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[8f5q]] is a 6 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=8F5Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8F5Q FirstGlance]. <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]] 1.9&#8491;</td></tr>
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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=8f5q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8f5q OCA], [https://pdbe.org/8f5q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8f5q RCSB], [https://www.ebi.ac.uk/pdbsum/8f5q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8f5q ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PCNA_HUMAN PCNA_HUMAN] Auxiliary protein of DNA polymerase delta and is involved in the control of eukaryotic DNA replication by increasing the polymerase's processibility during elongation of the leading strand. Induces a robust stimulatory effect on the 3'-5' exonuclease and 3'-phosphodiesterase, but not apurinic-apyrimidinic (AP) endonuclease, APEX2 activities. Has to be loaded onto DNA in order to be able to stimulate APEX2. Plays a key role in DNA damage response (DDR) by being conveniently positioned at the replication fork to coordinate DNA replication with DNA repair and DNA damage tolerance pathways. Acts as a loading platform to recruit DDR proteins that allow completion of DNA replication after DNA damage and promote postreplication repair: Monoubiquitinated PCNA leads to recruitment of translesion (TLS) polymerases, while 'Lys-63'-linked polyubiquitination of PCNA is involved in error-free pathway and employs recombination mechanisms to synthesize across the lesion.<ref>PMID:19443450</ref> <ref>PMID:18719106</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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F-box DNA helicase 1 (FBH1) is involved in the regulation of cell responses to replicative stress. FBH1 is recruited to stalled DNA replication fork by PCNA where it inhibits homologous recombination and catalyzes fork regression. Here, we report the structural basis for the molecular recognition of two distinctly different motifs of FBH1, FBH1(PIP) and FBH1(APIM), by PCNA. The crystal structure of PCNA in complex with FBH1(PIP) and analysis of NMR perturbations reveal overlapped FBH1(PIP) and FBH1(APIM) binding sites of PCNA and the dominant contribution of FBH1(PIP) in this interaction.
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Authors:
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Molecular insight into the PCNA-binding mode of FBH1.,Liu J, Chaves-Arquero B, Wei P, Tencer AH, Ruiz-Albor A, Zhang G, Blanco FJ, Kutateladze TG Structure. 2023 May 4;31(5):511-517.e3. doi: 10.1016/j.str.2023.03.004. Epub 2023 , Mar 28. PMID:36990095<ref>PMID:36990095</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 8f5q" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Blanco F]]
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[[Category: Chaves-Arquero B]]
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[[Category: Kutateladze T]]
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[[Category: Liu J]]
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[[Category: Tencer H]]
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[[Category: Wei P]]
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[[Category: Zhang G]]

Revision as of 06:57, 27 September 2023

Crystal structure of human PCNA in complex with the PIP box of FBH1

PDB ID 8f5q

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