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| | ==Crystal structure of ATBAG1 in complex with HSP70== | | ==Crystal structure of ATBAG1 in complex with HSP70== |
| - | <StructureSection load='4hwi' size='340' side='right' caption='[[4hwi]], [[Resolution|resolution]] 2.27Å' scene=''> | + | <StructureSection load='4hwi' size='340' side='right'caption='[[4hwi]], [[Resolution|resolution]] 2.27Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4hwi]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HWI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HWI FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4hwi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HWI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HWI FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4hwc|4hwc]], [[4hwd|4hwd]], [[4hwf|4hwf]], [[4hwh|4hwh]]</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=4hwi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hwi OCA], [https://pdbe.org/4hwi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hwi RCSB], [https://www.ebi.ac.uk/pdbsum/4hwi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hwi ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HSC70, HSP73, HSPA10, HSPA8 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), At5g52060, BAG1, MSG15.15 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr>
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| - | <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=4hwi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hwi OCA], [http://pdbe.org/4hwi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4hwi RCSB], [http://www.ebi.ac.uk/pdbsum/4hwi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4hwi ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/HSP7C_HUMAN HSP7C_HUMAN]] Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Chaperone. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex.<ref>PMID:10722728</ref> [[http://www.uniprot.org/uniprot/BAG1_ARATH BAG1_ARATH]] Co-chaperone that regulates diverse cellular pathways, such as programmed cell death and stress responses (By similarity). | + | [https://www.uniprot.org/uniprot/HSP7C_HUMAN HSP7C_HUMAN] Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Chaperone. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex.<ref>PMID:10722728</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[BAG protein|BAG protein]] | + | *[[BAG family proteins 3D structures|BAG family proteins 3D structures]] |
| | + | *[[Heat Shock Protein structures|Heat Shock Protein structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Arath]] | + | [[Category: Arabidopsis thaliana]] |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Fang, S]] | + | [[Category: Large Structures]] |
| - | [[Category: Shen, Y]] | + | [[Category: Fang S]] |
| - | [[Category: Bag domain]] | + | [[Category: Shen Y]] |
| - | [[Category: Chaperone-apoptosis complex]]
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| - | [[Category: Co-chaperone]]
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| - | [[Category: Complex with molecular chaperone]]
| + | |
| - | [[Category: Ubiquitin-like domain]]
| + | |
| Structural highlights
Function
HSP7C_HUMAN Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Chaperone. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex.[1]
Publication Abstract from PubMed
The recently identified plant Bcl-2-associated athanogene (BAG) family plays an extensive role in plant programmed cell death (PCD) processes ranging from growth and development to stress responses and even cell death. In the Arabidopsis thaliana BAG (AtBAG) protein family, four members (AtBAG1-4) have a domain organization similar to that of mammalian BAG proteins. Here, crystal structures of the BAG domains (BDs) of AtBAG1-4 have been determined; they have high homology and adopt a structure comprising three short parallel alpha-helices, similar to some mammalian BAG proteins. The crystal structure of a complex of the AtBAG1 ubiquitin-like domain and BAG domain (UBD) with the Hsc70 nucleotide-binding domain (NBD) was also determined. The binding of the AtBAG1 BD to the Hsc70 NBD induces conformational change of the Hsc70 NBD to the open state and reduces the affinity of the NBD for ADP. In vivo studies showed that bag2-1 mutant plants are larger than wild-type plants when growing under normal conditions, indicating that the AtBAG proteins might regulate plant PCD and confer tolerance to stresses in plants. These structural and functional analyses indicate that the AtBAG proteins function as nucleotide-exchange factors for Hsp70/Hsc70 in A. thaliana and that the mechanism of regulation of chaperone-mediated protein folding is conserved in plants.
Structural insight into plant programmed cell death mediated by BAG proteins in Arabidopsis thaliana.,Fang S, Li L, Cui B, Men S, Shen Y, Yang X Acta Crystallogr D Biol Crystallogr. 2013 Jun;69(Pt 6):934-45. doi:, 10.1107/S0907444913003624. Epub 2013 May 2. PMID:23695238[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Yahata T, de Caestecker MP, Lechleider RJ, Andriole S, Roberts AB, Isselbacher KJ, Shioda T. The MSG1 non-DNA-binding transactivator binds to the p300/CBP coactivators, enhancing their functional link to the Smad transcription factors. J Biol Chem. 2000 Mar 24;275(12):8825-34. PMID:10722728
- ↑ Fang S, Li L, Cui B, Men S, Shen Y, Yang X. Structural insight into plant programmed cell death mediated by BAG proteins in Arabidopsis thaliana. Acta Crystallogr D Biol Crystallogr. 2013 Jun;69(Pt 6):934-45. doi:, 10.1107/S0907444913003624. Epub 2013 May 2. PMID:23695238 doi:10.1107/S0907444913003624
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