4o0a: Difference between revisions

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<StructureSection load='4o0a' size='340' side='right' caption='[[4o0a]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
<StructureSection load='4o0a' size='340' side='right' caption='[[4o0a]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4o0a]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O0A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4O0A FirstGlance]. <br>
<table><tr><td colspan='2'>[[4o0a]] 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=4O0A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4O0A FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2P9:5-{4-[({[4-(5-CARBOXYFURAN-2-YL)-2-CHLOROPHENYL]CARBONOTHIOYL}AMINO)METHYL]PHENYL}-1-(3,4-DICHLOROPHENYL)-1H-PYRAZOLE-3-CARBOXYLIC+ACID'>2P9</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2P9:5-{4-[({[4-(5-CARBOXYFURAN-2-YL)-2-CHLOROPHENYL]CARBONOTHIOYL}AMINO)METHYL]PHENYL}-1-(3,4-DICHLOROPHENYL)-1H-PYRAZOLE-3-CARBOXYLIC+ACID'>2P9</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4luv|4luv]], [[4lwc|4lwc]], [[4lwi|4lwi]], [[4luz|4luz]], [[4luo|4luo]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4luv|4luv]], [[4lwc|4lwc]], [[4lwi|4lwi]], [[4luz|4luz]], [[4luo|4luo]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RPA1, REPA1, RPA70 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4o0a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o0a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4o0a RCSB], [http://www.ebi.ac.uk/pdbsum/4o0a PDBsum]</span></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=4o0a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o0a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4o0a RCSB], [http://www.ebi.ac.uk/pdbsum/4o0a PDBsum]</span></td></tr>
</table>
</table>
== Function ==
[[http://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> 


==See Also==
==See Also==
*[[Single-stranded DNA-binding protein|Single-stranded DNA-binding protein]]
*[[Single-stranded DNA-binding protein|Single-stranded DNA-binding protein]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Camper, D V.]]
[[Category: Human]]
[[Category: Chazin, W J.]]
[[Category: Camper, D V]]
[[Category: Feldkamp, M D.]]
[[Category: Chazin, W J]]
[[Category: Fesik, S W.]]
[[Category: Feldkamp, M D]]
[[Category: Frank, A O.]]
[[Category: Fesik, S W]]
[[Category: Kennedy, J P.]]
[[Category: Frank, A O]]
[[Category: Olejniczak, E T.]]
[[Category: Kennedy, J P]]
[[Category: Patrone, J D.]]
[[Category: Olejniczak, E T]]
[[Category: Pelz, N F.]]
[[Category: Patrone, J D]]
[[Category: Rossanese, O W.]]
[[Category: Pelz, N F]]
[[Category: Vangamudi, B.]]
[[Category: Rossanese, O W]]
[[Category: Waterson, A G.]]
[[Category: Vangamudi, B]]
[[Category: Waterson, A G]]
[[Category: Dna binding protein-inhibitor complex]]
[[Category: Dna binding protein-inhibitor complex]]
[[Category: Ob-fold]]
[[Category: Ob-fold]]
[[Category: Protein-protein interaction]]
[[Category: Protein-protein interaction]]

Revision as of 04:26, 25 December 2014

Fragment-Based Discovery of a Potent Inhibitor of Replication Protein A Protein-Protein InteractionsFragment-Based Discovery of a Potent Inhibitor of Replication Protein A Protein-Protein Interactions

Structural highlights

4o0a is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:RPA1, REPA1, RPA70 (HUMAN)
Resources:FirstGlance, OCA, RCSB, PDBsum

Function

[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.[1] [2] 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.[3] [4]

See Also

References

  1. Mason AC, Haring SJ, Pryor JM, Staloch CA, Gan TF, Wold MS. An alternative form of replication protein a prevents viral replication in vitro. J Biol Chem. 2009 Feb 20;284(8):5324-31. doi: 10.1074/jbc.M808963200. Epub 2008, Dec 29. PMID:19116208 doi:10.1074/jbc.M808963200
  2. Kemp MG, Mason AC, Carreira A, Reardon JT, Haring SJ, Borgstahl GE, Kowalczykowski SC, Sancar A, Wold MS. An alternative form of replication protein a expressed in normal human tissues supports DNA repair. J Biol Chem. 2010 Feb 12;285(7):4788-97. doi: 10.1074/jbc.M109.079418. Epub 2009 , Dec 7. PMID:19996105 doi:10.1074/jbc.M109.079418
  3. Mason AC, Haring SJ, Pryor JM, Staloch CA, Gan TF, Wold MS. An alternative form of replication protein a prevents viral replication in vitro. J Biol Chem. 2009 Feb 20;284(8):5324-31. doi: 10.1074/jbc.M808963200. Epub 2008, Dec 29. PMID:19116208 doi:10.1074/jbc.M808963200
  4. Kemp MG, Mason AC, Carreira A, Reardon JT, Haring SJ, Borgstahl GE, Kowalczykowski SC, Sancar A, Wold MS. An alternative form of replication protein a expressed in normal human tissues supports DNA repair. J Biol Chem. 2010 Feb 12;285(7):4788-97. doi: 10.1074/jbc.M109.079418. Epub 2009 , Dec 7. PMID:19996105 doi:10.1074/jbc.M109.079418

4o0a, resolution 1.20Å

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