3ldn
From Proteopedia
(Difference between revisions)
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- | + | ==Crystal structure of human GRP78 (70kDa heat shock protein 5 / BIP) ATPase domain in apo form== | |
- | + | <StructureSection load='3ldn' size='340' side='right' caption='[[3ldn]], [[Resolution|resolution]] 2.20Å' scene=''> | |
- | + | == Structural highlights == | |
+ | <table><tr><td colspan='2'>[[3ldn]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LDN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LDN FirstGlance]. <br> | ||
+ | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ldl|3ldl]], [[3ldo|3ldo]], [[3ldp|3ldp]], [[3ldq|3ldq]]</td></tr> | ||
+ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HSPA5, GRP78 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=3ldn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ldn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ldn RCSB], [http://www.ebi.ac.uk/pdbsum/3ldn PDBsum]</span></td></tr> | ||
+ | </table> | ||
+ | == Disease == | ||
+ | [[http://www.uniprot.org/uniprot/GRP78_HUMAN GRP78_HUMAN]] Note=Autoantigen in rheumatoid arthritis.<ref>PMID:11160188</ref> | ||
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/GRP78_HUMAN GRP78_HUMAN]] Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER.<ref>PMID:2294010</ref> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == 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<ref>PMID:21526763</ref> | |
- | + | ||
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | == References == | |
- | == | + | <references/> |
- | + | __TOC__ | |
- | + | </StructureSection> | |
- | + | ||
- | + | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
- | [[Category: Dokurno, P | + | [[Category: Dokurno, P]] |
- | [[Category: Macias, A T | + | [[Category: Macias, A T]] |
- | [[Category: Massey, A J | + | [[Category: Massey, A J]] |
- | [[Category: Shaw, T | + | [[Category: Shaw, T]] |
- | [[Category: Surgenor, A E | + | [[Category: Surgenor, A E]] |
- | [[Category: Williamson, D S | + | [[Category: Williamson, D S]] |
[[Category: Adenosine]] | [[Category: Adenosine]] | ||
[[Category: Atp-binding]] | [[Category: Atp-binding]] |
Revision as of 14:58, 18 December 2014
Crystal structure of human GRP78 (70kDa heat shock protein 5 / BIP) ATPase domain in apo form
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Categories: Homo sapiens | Dokurno, P | Macias, A T | Massey, A J | Shaw, T | Surgenor, A E | Williamson, D S | Adenosine | Atp-binding | Chaperone | Endoplasmic reticulum | Grp78 | Heat shock | Hsc70 | Hsp70 | Nucleoside | Nucleotide-binding | Phosphoprotein | Protein folding | Selectivity | Small molecule inhibitor | Stress response