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| | <StructureSection load='1ud0' size='340' side='right'caption='[[1ud0]], [[Resolution|resolution]] 3.45Å' scene=''> | | <StructureSection load='1ud0' size='340' side='right'caption='[[1ud0]], [[Resolution|resolution]] 3.45Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1ud0]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UD0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UD0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1ud0]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UD0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UD0 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.45Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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=1ud0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ud0 OCA], [http://pdbe.org/1ud0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ud0 RCSB], [http://www.ebi.ac.uk/pdbsum/1ud0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ud0 ProSAT]</span></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=1ud0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ud0 OCA], [https://pdbe.org/1ud0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ud0 RCSB], [https://www.ebi.ac.uk/pdbsum/1ud0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ud0 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/HSP7C_RAT HSP7C_RAT]] 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 (By similarity). | + | [https://www.uniprot.org/uniprot/HSP7C_RAT HSP7C_RAT] 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 (By similarity). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Buffalo rat]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chou, C C]] | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Forouhar, F]] | + | [[Category: Chou CC]] |
| - | [[Category: Hsiao, C D]] | + | [[Category: Forouhar F]] |
| - | [[Category: Wang, C]] | + | [[Category: Hsiao CD]] |
| - | [[Category: Yeh, Y H]] | + | [[Category: Wang C]] |
| - | [[Category: Chaperone]]
| + | [[Category: Yeh YH]] |
| - | [[Category: Hsc70]]
| + | |
| Structural highlights
Function
HSP7C_RAT 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 (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The 70-kDa heat shock proteins (Hsp70), including the cognates (Hsc70), are molecular chaperones that prevent misfolding and aggregation of polypeptides in cells under both normal and stressed conditions. They are composed of two major structural domains: an N-terminal 44-kDa ATPase domain and a C-terminal 30-kDa substrate binding domain. The 30-kDa domain can be divided into an 18-kDa subdomain and a 10-kDa subdomain. Here we report the crystal structure of the 10-kDa subdomain of rat Hsc70 at 3.45 A. Its helical region adopted a helix-loop-helix fold. This conformation is different from the equivalent subdomain of DnaK, the bacterial homologue of Hsc70. Moreover, in the crystalline state, the 10-kDa subdomain formed dimers. The results of gel filtration chromatography further supported the view that this subdomain was self-associated. Upon gel filtration, Hsc70 was found to exist as a mixture of monomers, dimers, and oligomers, but the 60-kDa fragment was predominantly found to exist as monomers. These findings suggest that the alpha-helical region of the 10-kDa subdomain dictates the chaperone self-association.
Crystal structure of the C-terminal 10-kDa subdomain of Hsc70.,Chou CC, Forouhar F, Yeh YH, Shr HL, Wang C, Hsiao CD J Biol Chem. 2003 Aug 8;278(32):30311-6. Epub 2003 May 28. PMID:12773536[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chou CC, Forouhar F, Yeh YH, Shr HL, Wang C, Hsiao CD. Crystal structure of the C-terminal 10-kDa subdomain of Hsc70. J Biol Chem. 2003 Aug 8;278(32):30311-6. Epub 2003 May 28. PMID:12773536 doi:10.1074/jbc.M304563200
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