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1axc

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[[Image:1axc.gif|left|200px]]
 
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{{Structure
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==HUMAN PCNA==
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|PDB= 1axc |SIZE=350|CAPTION= <scene name='initialview01'>1axc</scene>, resolution 2.6&Aring;
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<StructureSection load='1axc' size='340' side='right'caption='[[1axc]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1axc]] 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=1AXC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AXC FirstGlance]. <br>
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|ACTIVITY=
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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]] 2.6&#8491;</td></tr>
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|GENE=
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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=1axc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1axc OCA], [https://pdbe.org/1axc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1axc RCSB], [https://www.ebi.ac.uk/pdbsum/1axc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1axc ProSAT]</span></td></tr>
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}}
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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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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ax/1axc_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</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/main_output.php?pdb_ID=1axc ConSurf].
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<div style="clear:both"></div>
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'''HUMAN PCNA'''
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==See Also==
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*[[Proliferating cell nuclear antigen 3D structures|Proliferating cell nuclear antigen 3D structures]]
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== References ==
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==Overview==
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<references/>
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The crystal structure of the human DNA polymerase delta processivity factor PCNA (proliferating cell nuclear antigen) complexed with a 22 residue peptide derived from the C-terminus of the cell-cycle checkpoint protein p21(WAF1/CIP1) has been determined at 2.6 angstrom resolution. p21 binds to PCNA in a 1:1 stoichiometry with an extensive array of interactions that include the formation of a beta sheet with the interdomain connector loop of PCNA. An intact trimeric ring is maintained in the structure of the p21-PCNA complex, with a central hole available for DNA interaction. The ability of p21 to inhibit the action of PCNA is therefore likely to be due to its masking of elements on PCNA that are required for the binding of other components of the polymerase assembly.
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__TOC__
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</StructureSection>
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==Disease==
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Known disease associated with this structure: Multiple endocrine neoplasia, type IV OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=600778 600778]]
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==About this Structure==
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1AXC is a [[Protein complex]] structure of sequences 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=1AXC OCA].
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==Reference==
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Structure of the C-terminal region of p21(WAF1/CIP1) complexed with human PCNA., Gulbis JM, Kelman Z, Hurwitz J, O'Donnell M, Kuriyan J, Cell. 1996 Oct 18;87(2):297-306. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8861913 8861913]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Gulbis, J M.]]
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[[Category: Gulbis JM]]
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[[Category: Kuriyan, J.]]
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[[Category: Kuriyan J]]
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[[Category: cip1]]
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[[Category: complex (dna-binding protein/dna)]]
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[[Category: dna]]
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[[Category: oncogene]]
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[[Category: processivity]]
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[[Category: replication]]
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[[Category: waf1]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:03:25 2008''
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Current revision

HUMAN PCNA

PDB ID 1axc

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