4o0a: Difference between revisions
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<StructureSection load='4o0a' size='340' side='right' caption='[[4o0a]], [[Resolution|resolution]] 1.20Å' scene=''> | <StructureSection load='4o0a' size='340' side='right' caption='[[4o0a]], [[Resolution|resolution]] 1.20Å' 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
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 AlsoReferences
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