2b29

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(New page: 200px<br /> <applet load="2b29" size="450" color="white" frame="true" align="right" spinBox="true" caption="2b29, resolution 1.60&Aring;" /> '''N-terminal domain o...)
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[[Image:2b29.gif|left|200px]]<br />
 
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<applet load="2b29" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2b29, resolution 1.60&Aring;" />
 
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'''N-terminal domain of the RPA70 subunit of human replication protein A.'''<br />
 
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==Overview==
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==N-terminal domain of the RPA70 subunit of human replication protein A.==
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One of many protein-protein interactions modulated upon DNA damage is that, of the single-stranded DNA-binding protein, replication protein A (RPA), with the p53 tumor suppressor. Here we report the crystal structure of RPA, residues 1-120 (RPA70N) bound to the N-terminal transactivation domain of, p53 (residues 37-57; p53N) and, by using NMR spectroscopy, characterize, two mechanisms by which the RPA/p53 interaction can be modulated. RPA70N, forms an oligonucleotide/oligosaccharide-binding fold, similar to that, previously observed for the ssDNA-binding domains of RPA. In contrast, the, N-terminal p53 transactivation domain is largely disordered in solution, but residues 37-57 fold into two amphipathic helices, H1 and H2, upon, binding with RPA70N. The H2 helix of p53 structurally mimics the binding, of ssDNA to the oligonucleotide/oligosaccharide-binding fold. NMR, experiments confirmed that both ssDNA and an acidic peptide mimicking a, phosphorylated form of RPA32N can independently compete the acidic p53N, out of the binding site. Taken together, our data suggest a mechanism for, DNA damage signaling that can explain a threshold response to DNA damage.
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<StructureSection load='2b29' size='340' side='right'caption='[[2b29]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2b29]] 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=2B29 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2B29 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]] 1.6&#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=2b29 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b29 OCA], [https://pdbe.org/2b29 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b29 RCSB], [https://www.ebi.ac.uk/pdbsum/2b29 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b29 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RFA1_HUMAN RFA1_HUMAN] Plays an essential role in several cellular processes in DNA metabolism including replication, recombination and DNA repair. Binds and subsequently stabilizes single-stranded DNA intermediates and thus prevents complementary DNA from reannealing.<ref>PMID:19116208</ref> <ref>PMID:19996105</ref> Functions as component of the alternative replication protein A complex (aRPA). aRPA binds single-stranded DNA and probably plays a role in DNA repair; it does not support chromosomal DNA replication and cell cycle progression through S-phase. In vitro, aRPA cannot promote efficient priming by DNA polymerase alpha but supports DNA polymerase delta synthesis in the presence of PCNA and replication factor C (RFC), the dual incision/excision reaction of nucleotide excision repair and RAD51-dependent strand exchange.<ref>PMID:19116208</ref> <ref>PMID:19996105</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/b2/2b29_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=2b29 ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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2B29 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2B29 OCA].
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*[[Single-stranded DNA-binding protein 3D structures|Single-stranded DNA-binding protein 3D structures]]
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== References ==
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==Reference==
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<references/>
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Single-stranded DNA mimicry in the p53 transactivation domain interaction with replication protein A., Bochkareva E, Kaustov L, Ayed A, Yi GS, Lu Y, Pineda-Lucena A, Liao JC, Okorokov AL, Milner J, Arrowsmith CH, Bochkarev A, Proc Natl Acad Sci U S A. 2005 Oct 25;102(43):15412-7. Epub 2005 Oct 17. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16234232 16234232]
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Arrowsmith, C.H.]]
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[[Category: Arrowsmith CH]]
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[[Category: Ayed, A.]]
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[[Category: Ayed A]]
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[[Category: Bochkarev, A.]]
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[[Category: Bochkarev A]]
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[[Category: Bochkareva, E.]]
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[[Category: Bochkareva E]]
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[[Category: Kaustov, L.]]
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[[Category: Kaustov L]]
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[[Category: Milner, J.]]
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[[Category: Milner J]]
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[[Category: Okorokov, A.]]
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[[Category: Okorokov A]]
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[[Category: replication]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:57:28 2007''
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Current revision

N-terminal domain of the RPA70 subunit of human replication protein A.

PDB ID 2b29

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