6heq

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 3: Line 3:
<StructureSection load='6heq' size='340' side='right'caption='[[6heq]], [[Resolution|resolution]] 1.23&Aring;' scene=''>
<StructureSection load='6heq' size='340' side='right'caption='[[6heq]], [[Resolution|resolution]] 1.23&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[6heq]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HEQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HEQ FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[6heq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arabian_camel Arabian camel]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HEQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HEQ FirstGlance]. <br>
</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=6heq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6heq OCA], [http://pdbe.org/6heq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6heq RCSB], [http://www.ebi.ac.uk/pdbsum/6heq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6heq ProSAT]</span></td></tr>
</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=6heq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6heq OCA], [http://pdbe.org/6heq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6heq RCSB], [http://www.ebi.ac.uk/pdbsum/6heq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6heq ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
-
Prion disorders are infectious diseases that are characterized by the conversion of the cellular prion protein PrPC into the pathogenic isoform PrPSc. Specific antibodies that interact with the cellular prion protein have been shown to inhibit this transition. Recombinant VHHs (variable domain of dromedary heavy-chain antibodies) or nanobodies are single-domain antibodies, making them the smallest antigen-binding fragments. A specific nanobody (Nb_PrP_01) was raised against mouse PrPC. A crystallization condition for this recombinant nanobody was identified using high-throughput screening. The crystals were optimized using streak-seeding and the hanging-drop method. The crystals belonged to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a=30.04, b=37.15, c=83.00 A, and diffracted to 1.23 A resolution using synchrotron radiation. The crystal structure of this specific nanobody against PrPC together with the known PrPC structure may help in understanding the PrPC/PrPSc transition mechanism.
+
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.
-
Crystallization and preliminary X-ray diffraction analysis of a specific VHH domain against mouse prion protein.,Abskharon RN, Soror SH, Pardon E, El Hassan H, Legname G, Steyaert J, Wohlkonig A Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Dec 1;66(Pt 12):1644-6., doi: 10.1107/S1744309110042168. Epub 2010 Nov 26. PMID:21139215<ref>PMID:21139215</ref>
+
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>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Line 19: Line 19:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
 +
[[Category: Arabian camel]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Abskharon, R N]]
[[Category: Abskharon, R N]]

Revision as of 10:40, 18 December 2019

Prion nanobody 484

PDB ID 6heq

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6heq"
Personal tools