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4mqv

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==Crystal complex of Rpa32c and Smarcal1 N-terminus==
==Crystal complex of Rpa32c and Smarcal1 N-terminus==
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<StructureSection load='4mqv' size='340' side='right' caption='[[4mqv]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
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<StructureSection load='4mqv' size='340' side='right'caption='[[4mqv]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4mqv]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MQV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MQV FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4mqv]] is a 4 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=4MQV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MQV FirstGlance]. <br>
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</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=4mqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mqv OCA], [http://pdbe.org/4mqv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4mqv RCSB], [http://www.ebi.ac.uk/pdbsum/4mqv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4mqv ProSAT]</span></td></tr>
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</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=4mqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mqv OCA], [https://pdbe.org/4mqv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mqv RCSB], [https://www.ebi.ac.uk/pdbsum/4mqv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mqv ProSAT]</span></td></tr>
</table>
</table>
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== Disease ==
 
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[[http://www.uniprot.org/uniprot/SMAL1_HUMAN SMAL1_HUMAN]] Schimke immuno-osseous dysplasia. The disease is caused by mutations affecting the gene represented in this entry.
 
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/RFA2_HUMAN RFA2_HUMAN]] Required for DNA recombination, repair and replication. The activity of RP-A is mediated by single-stranded DNA binding and protein interactions. Required for the efficient recruitment of the DNA double-strand break repair factor RAD51 to chromatin in response to DNA damage.<ref>PMID:15205463</ref> <ref>PMID:19116208</ref> <ref>PMID:19996105</ref> <ref>PMID:20154705</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:15205463</ref> <ref>PMID:19116208</ref> <ref>PMID:19996105</ref> <ref>PMID:20154705</ref> [[http://www.uniprot.org/uniprot/SMAL1_HUMAN SMAL1_HUMAN]] ATP-dependent annealing helicase that catalyzes the rewinding of the stably unwound DNA. Rewinds single-stranded DNA bubbles that are stably bound by replication protein A (RPA). Acts throughout the genome to reanneal stably unwound DNA, performing the opposite reaction of many enzymes, such as helicases and polymerases, that unwind DNA.<ref>PMID:18974355</ref>
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[https://www.uniprot.org/uniprot/RFA2_HUMAN RFA2_HUMAN] Required for DNA recombination, repair and replication. The activity of RP-A is mediated by single-stranded DNA binding and protein interactions. Required for the efficient recruitment of the DNA double-strand break repair factor RAD51 to chromatin in response to DNA damage.<ref>PMID:15205463</ref> <ref>PMID:19116208</ref> <ref>PMID:19996105</ref> <ref>PMID:20154705</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:15205463</ref> <ref>PMID:19116208</ref> <ref>PMID:19996105</ref> <ref>PMID:20154705</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Qian, C M]]
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[[Category: Homo sapiens]]
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[[Category: Xie, S]]
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[[Category: Large Structures]]
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[[Category: Nucleus]]
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[[Category: Qian CM]]
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[[Category: Protein binding]]
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[[Category: Xie S]]
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[[Category: Winged hth fold]]
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Current revision

Crystal complex of Rpa32c and Smarcal1 N-terminus

PDB ID 4mqv

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