6hhd: Difference between revisions

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OCA

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-'''Unreleased structure'''
-The entry 6hhd is ON HOLD
+==Mouse Prion Protein in complex with Nanobody 484==
+<StructureSection load='6hhd' size='340' side='right'caption='[[6hhd]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6hhd]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Arabian_camel Arabian camel] and [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HHD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HHD FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Prnp, Prn-p, Prp ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=6hhd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hhd OCA], [http://pdbe.org/6hhd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hhd RCSB], [http://www.ebi.ac.uk/pdbsum/6hhd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hhd ProSAT]</span></td></tr>
+</table>
+== Disease ==
+[[http://www.uniprot.org/uniprot/PRIO_MOUSE PRIO_MOUSE]] Note=Found in high quantity in the brain of humans and animals infected with degenerative neurological diseases such as kuru, Creutzfeldt-Jakob disease (CJD), Gerstmann-Straussler syndrome (GSS), scrapie, bovine spongiform encephalopathy (BSE), transmissible mink encephalopathy (TME), etc.
+== Function ==
+[[http://www.uniprot.org/uniprot/PRIO_MOUSE PRIO_MOUSE]] May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May play a role in iron uptake and iron homeostasis. Soluble oligomers are toxic to cultured neuroblastoma cells and induce apoptosis (in vitro) (By similarity). Association with GPC1 (via its heparan sulfate chains) targets PRNP to lipid rafts. Also provides Cu(2+) or ZN(2+) for the ascorbate-mediated GPC1 deaminase degradation of its heparan sulfate side chains.<ref>PMID:12732622</ref> <ref>PMID:16492732</ref> <ref>PMID:19242475</ref> <ref>PMID:19568430</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Prion or PrPSc is the proteinaceous infectious agent causing prion diseases in various mammalian species. Despite decades of research, the structural basis for PrPSc formation and prion infectivity remains elusive. To understand the role of the hydrophobic region in forming infectious prion at the molecular level, we report X-ray crystal structures of mouse (Mo) prion protein (PrP) (residues 89-230) in complex with a nanobody (Nb484). Using the recombinant prion propagation system, we show that the binding of Nb484 to the hydrophobic region of MoPrP efficiently inhibits the propagation of proteinase K resistant PrPSc and prion infectivity. In addition, when added to cultured mouse brain slices in high concentrations, Nb484 exhibits no neurotoxicity, which is drastically different from other neurotoxic anti-PrP antibodies, suggesting that the Nb484 can be a potential therapeutic agent against prion disease. In summary, our data provides the first structure-function evidence supporting a crucial role of the hydrophobic region of PrP in forming an infectious prion.
-Authors: Soror, S., Abskharon, R., Wohlkonig, A.
+Structural evidence for the critical role of the prion protein hydrophobic region in forming an infectious prion.,Abskharon R, Wang F, Wohlkonig A, Ruan J, Soror S, Giachin G, Pardon E, Zou W, Legname G, Ma J, Steyaert J PLoS Pathog. 2019 Dec 9;15(12):e1008139. doi: 10.1371/journal.ppat.1008139. PMID:31815959<ref>PMID:31815959</ref>
-Description: Mouse Prion Protein in complex with Nanobody 484
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Wohlkonig, A]]
+<div class="pdbe-citations 6hhd" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Arabian camel]]
+[[Category: Large Structures]]
+[[Category: Lk3 transgenic mice]]
 [[Category: Abskharon, R]]
 [[Category: Soror, S]]
+[[Category: Wohlkonig, A]]
+[[Category: Aggregation]]
+[[Category: B-sheet]]
+[[Category: Nanobody]]
+[[Category: Prion]]
+[[Category: Protein binding]]