4mqv
From Proteopedia
(Difference between revisions)
(One intermediate revision not shown.) | |||
Line 3: | Line 3: | ||
<StructureSection load='4mqv' size='340' side='right'caption='[[4mqv]], [[Resolution|resolution]] 1.95Å' scene=''> | <StructureSection load='4mqv' size='340' side='right'caption='[[4mqv]], [[Resolution|resolution]] 1.95Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[4mqv]] is a 4 chain structure with sequence from [ | + | <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> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95Å</td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <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> | ||
- | == Disease == | ||
- | [[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 == | ||
- | [ | + | [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 == | ||
Line 24: | Line 22: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: | + | [[Category: Homo sapiens]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Qian | + | [[Category: Qian CM]] |
- | [[Category: Xie | + | [[Category: Xie S]] |
- | + | ||
- | + | ||
- | + |
Current revision
Crystal complex of Rpa32c and Smarcal1 N-terminus
|