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| | <StructureSection load='3ldq' size='340' side='right'caption='[[3ldq]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='3ldq' size='340' side='right'caption='[[3ldq]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3ldq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LDQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LDQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3ldq]] is a 2 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=3LDQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LDQ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3P1:8-[(QUINOLIN-2-YLMETHYL)AMINO]ADENOSINE'>3P1</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]] 1.9Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3ldl|3ldl]], [[3ldn|3ldn]], [[3ldo|3ldo]], [[3ldp|3ldp]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3P1:8-[(QUINOLIN-2-YLMETHYL)AMINO]ADENOSINE'>3P1</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HSPA8, HSC70, HSP73, HSPA10 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), BAG1, HAP ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3ldq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ldq OCA], [https://pdbe.org/3ldq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ldq RCSB], [https://www.ebi.ac.uk/pdbsum/3ldq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ldq 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=3ldq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ldq OCA], [https://pdbe.org/3ldq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ldq RCSB], [https://www.ebi.ac.uk/pdbsum/3ldq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ldq ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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> [[https://www.uniprot.org/uniprot/BAG1_HUMAN BAG1_HUMAN]] Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release. Inhibits the pro-apoptotic function of PPP1R15A, and has anti-apoptotic activity. Markedly increases the anti-cell death function of BCL2 induced by various stimuli.<ref>PMID:9305631</ref> <ref>PMID:9873016</ref> <ref>PMID:12724406</ref>
| + | [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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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Dokurno, P]] | + | [[Category: Dokurno P]] |
| - | [[Category: Macias, A T]] | + | [[Category: Macias AT]] |
| - | [[Category: Massey, A J]] | + | [[Category: Massey AJ]] |
| - | [[Category: Shaw, T]] | + | [[Category: Shaw T]] |
| - | [[Category: Surgenor, A E]] | + | [[Category: Surgenor AE]] |
| - | [[Category: Williamson, D S]] | + | [[Category: Williamson DS]] |
| - | [[Category: Adenosine]]
| + | |
| - | [[Category: Apoptosis]]
| + | |
| - | [[Category: Atp-binding]]
| + | |
| - | [[Category: Chaperone]]
| + | |
| - | [[Category: Grp78]]
| + | |
| - | [[Category: Heat shock]]
| + | |
| - | [[Category: Hsc70]]
| + | |
| - | [[Category: Hsp70]]
| + | |
| - | [[Category: Nucleoside]]
| + | |
| - | [[Category: Nucleotide-binding]]
| + | |
| - | [[Category: Nucleus]]
| + | |
| - | [[Category: Phosphoprotein]]
| + | |
| - | [[Category: Protein folding]]
| + | |
| - | [[Category: Selectivity]]
| + | |
| - | [[Category: Small molecule inhibitor]]
| + | |
| - | [[Category: Stress response]]
| + | |
| 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
78 kDa glucose-regulated protein (Grp78) is a heat shock protein (HSP) involved in protein folding that plays a role in cancer cell proliferation. Binding of adenosine-derived inhibitors to Grp78 was characterized by surface plasmon resonance and isothermal titration calorimetry. The most potent compounds were 13 (VER-155008) with K(D) = 80 nM and 14 with K(D) = 60 nM. X-ray crystal structures of Grp78 bound to ATP, ADPnP, and adenosine derivative 10 revealed differences in the binding site between Grp78 and homologous proteins.
Adenosine-Derived Inhibitors of 78 kDa Glucose Regulated Protein (Grp78) ATPase: Insights into Isoform Selectivity.,Macias AT, Williamson DS, Allen N, Borgognoni J, Clay A, Daniels Z, Dokurno P, Drysdale MJ, Francis GL, Graham CJ, Howes R, Matassova N, Murray JB, Parsons R, Shaw T, Surgenor AE, Terry L, Wang Y, Wood M, Massey AJ J Med Chem. 2011 May 20. PMID:21526763[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
- ↑ Macias AT, Williamson DS, Allen N, Borgognoni J, Clay A, Daniels Z, Dokurno P, Drysdale MJ, Francis GL, Graham CJ, Howes R, Matassova N, Murray JB, Parsons R, Shaw T, Surgenor AE, Terry L, Wang Y, Wood M, Massey AJ. Adenosine-Derived Inhibitors of 78 kDa Glucose Regulated Protein (Grp78) ATPase: Insights into Isoform Selectivity. J Med Chem. 2011 May 20. PMID:21526763 doi:10.1021/jm101625x
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