4ipc: Difference between revisions

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==Structure of the N-terminal domain of RPA70, E7R mutant==
==Structure of the N-terminal domain of RPA70, E7R mutant==
<StructureSection load='4ipc' size='340' side='right' caption='[[4ipc]], [[Resolution|resolution]] 1.22&Aring;' scene=''>
<StructureSection load='4ipc' size='340' side='right'caption='[[4ipc]], [[Resolution|resolution]] 1.22&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4ipc]] 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=4IPC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4IPC FirstGlance]. <br>
<table><tr><td colspan='2'>[[4ipc]] 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=4IPC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IPC FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ipd|4ipd]], [[4ipg|4ipg]], [[4iph|4iph]]</td></tr>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ipc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ipc OCA], [https://pdbe.org/4ipc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ipc RCSB], [https://www.ebi.ac.uk/pdbsum/4ipc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ipc ProSAT]</span></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=4ipc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ipc OCA], [http://pdbe.org/4ipc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ipc RCSB], [http://www.ebi.ac.uk/pdbsum/4ipc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ipc ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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>
[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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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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==See Also==
==See Also==
*[[Single-stranded DNA-binding protein|Single-stranded DNA-binding protein]]
*[[Single-stranded DNA-binding protein 3D structures|Single-stranded DNA-binding protein 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Chazin, W J]]
[[Category: Large Structures]]
[[Category: Feldkamp, M D]]
[[Category: Chazin WJ]]
[[Category: Fesik, S W]]
[[Category: Feldkamp MD]]
[[Category: Frank, A O]]
[[Category: Fesik SW]]
[[Category: Vangamudi, B]]
[[Category: Frank AO]]
[[Category: Ob-fold]]
[[Category: Vangamudi B]]
[[Category: Protein binding]]

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