3we3: Difference between revisions
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{{STRUCTURE_3we3| PDB=3we3 | SCENE= }} | {{STRUCTURE_3we3| PDB=3we3 | SCENE= }} | ||
===Structure of BLM RQC domain bound to an arsenate ion=== | ===Structure of BLM RQC domain bound to an arsenate ion=== | ||
{{ABSTRACT_PUBMED_24257077}} | |||
==Disease== | ==Disease== | ||
Line 9: | Line 10: | ||
==About this Structure== | ==About this Structure== | ||
[[3we3]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WE3 OCA]. | [[3we3]] is a 2 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=3WE3 OCA]. | ||
==Reference== | ==Reference== | ||
<references group="xtra"/><references/> | <ref group="xtra">PMID:024257077</ref><references group="xtra"/><references/> | ||
[[Category: DNA helicase]] | [[Category: DNA helicase]] | ||
[[Category: Human]] | |||
[[Category: Hakoshima, T.]] | |||
[[Category: Kim, S Y.]] | |||
[[Category: Kitano, K.]] | [[Category: Kitano, K.]] | ||
[[Category: Dna binding]] | [[Category: Dna binding]] |
Revision as of 09:19, 4 December 2013
Structure of BLM RQC domain bound to an arsenate ionStructure of BLM RQC domain bound to an arsenate ion
Template:ABSTRACT PUBMED 24257077
DiseaseDisease
[BLM_HUMAN] Bloom syndrome. The disease is caused by mutations affecting the gene represented in this entry.
FunctionFunction
[BLM_HUMAN] Participates in DNA replication and repair. Exhibits a magnesium-dependent ATP-dependent DNA-helicase activity that unwinds single- and double-stranded DNA in a 3'-5' direction. Involved in 5'-end resection of DNA during double-strand break (DSB) repair: unwinds DNA and recruits DNA2 which mediates the cleavage of 5'-ssDNA. Negatively regulates sister chromatid exchange (SCE).[1] [2] [3] [4]
About this StructureAbout this Structure
3we3 is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ Kim SY, Hakoshima T, Kitano K. Structure of the RecQ C-terminal Domain of Human Bloom Syndrome Protein. Sci Rep. 2013 Nov 21;3:3294. doi: 10.1038/srep03294. PMID:24257077 doi:http://dx.doi.org/10.1038/srep03294
- ↑ Karow JK, Chakraverty RK, Hickson ID. The Bloom's syndrome gene product is a 3'-5' DNA helicase. J Biol Chem. 1997 Dec 5;272(49):30611-4. PMID:9388193
- ↑ Langland G, Elliott J, Li Y, Creaney J, Dixon K, Groden J. The BLM helicase is necessary for normal DNA double-strand break repair. Cancer Res. 2002 May 15;62(10):2766-70. PMID:12019152
- ↑ Nimonkar AV, Genschel J, Kinoshita E, Polaczek P, Campbell JL, Wyman C, Modrich P, Kowalczykowski SC. BLM-DNA2-RPA-MRN and EXO1-BLM-RPA-MRN constitute two DNA end resection machineries for human DNA break repair. Genes Dev. 2011 Feb 15;25(4):350-62. doi: 10.1101/gad.2003811. PMID:21325134 doi:http://dx.doi.org/10.1101/gad.2003811
- ↑ Wan L, Han J, Liu T, Dong S, Xie F, Chen H, Huang J. Scaffolding protein SPIDR/KIAA0146 connects the Bloom syndrome helicase with homologous recombination repair. Proc Natl Acad Sci U S A. 2013 Jun 25;110(26):10646-51. doi:, 10.1073/pnas.1220921110. Epub 2013 Mar 18. PMID:23509288 doi:http://dx.doi.org/10.1073/pnas.1220921110