3o79: Difference between revisions

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[[Image:3o79.png|left|200px]]


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==Crystal Structure of Wild-type Rabbit PrP 126-230==
The line below this paragraph, containing "STRUCTURE_3o79", creates the "Structure Box" on the page.
<StructureSection load='3o79' size='340' side='right'caption='[[3o79]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[3o79]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O79 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3O79 FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
{{STRUCTURE_3o79|  PDB=3o79  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3o79 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o79 OCA], [https://pdbe.org/3o79 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3o79 RCSB], [https://www.ebi.ac.uk/pdbsum/3o79 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3o79 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9TSF8_RABIT Q9TSF8_RABIT]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Prion diseases occur when the normally alpha-helical prion protein (PrP) converts to a pathological beta-structured state with prion infectivity (PrP(Sc)). Exposure to PrP(Sc) from other mammals can catalyze this conversion. Evidence from experimental and accidental transmission of prions suggests that mammals vary in their prion disease susceptibility: Hamsters and mice show relatively high susceptibility, whereas rabbits, horses, and dogs show low susceptibility. Using a novel approach to quantify conformational states of PrP by circular dichroism (CD), we find that prion susceptibility tracks with the intrinsic propensity of mammalian PrP to convert from the native, alpha-helical state to a cytotoxic beta-structured state, which exists in a monomer-octamer equilibrium. It has been controversial whether beta-structured monomers exist at acidic pH; sedimentation equilibrium and dual-wavelength CD evidence is presented for an equilibrium between a beta-structured monomer and octamer in some acidic pH conditions. Our X-ray crystallographic structure of rabbit PrP has identified a key helix-capping motif implicated in the low prion disease susceptibility of rabbits. Removal of this capping motif increases the beta-structure folding propensity of rabbit PrP to match that of PrP from mouse, a species more susceptible to prion disease.


===Crystal Structure of Wild-type Rabbit PrP 126-230===
Prion disease susceptibility is affected by {beta}-structure folding propensity and local side-chain interactions in PrP.,Khan MQ, Sweeting B, Mulligan VK, Arslan PE, Cashman NR, Pai EF, Chakrabartty A Proc Natl Acad Sci U S A. 2010 Nov 16;107(46):19808-19813. Epub 2010 Nov, 1. PMID:21041683<ref>PMID:21041683</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3o79" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_21041683}}, adds the Publication Abstract to the page
*[[Prion 3D structures|Prion 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 21041683 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_21041683}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
[[3o79]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O79 OCA].
 
==Reference==
<ref group="xtra">PMID:21041683</ref><references group="xtra"/>
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
[[Category: Chakrabartty, A.]]
[[Category: Chakrabartty A]]
[[Category: Pai, E F.]]
[[Category: Pai EF]]
[[Category: Sweeting, B.]]
[[Category: Sweeting B]]

Latest revision as of 09:02, 17 October 2024

Crystal Structure of Wild-type Rabbit PrP 126-230Crystal Structure of Wild-type Rabbit PrP 126-230

Structural highlights

3o79 is a 2 chain structure with sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.6Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q9TSF8_RABIT

Publication Abstract from PubMed

Prion diseases occur when the normally alpha-helical prion protein (PrP) converts to a pathological beta-structured state with prion infectivity (PrP(Sc)). Exposure to PrP(Sc) from other mammals can catalyze this conversion. Evidence from experimental and accidental transmission of prions suggests that mammals vary in their prion disease susceptibility: Hamsters and mice show relatively high susceptibility, whereas rabbits, horses, and dogs show low susceptibility. Using a novel approach to quantify conformational states of PrP by circular dichroism (CD), we find that prion susceptibility tracks with the intrinsic propensity of mammalian PrP to convert from the native, alpha-helical state to a cytotoxic beta-structured state, which exists in a monomer-octamer equilibrium. It has been controversial whether beta-structured monomers exist at acidic pH; sedimentation equilibrium and dual-wavelength CD evidence is presented for an equilibrium between a beta-structured monomer and octamer in some acidic pH conditions. Our X-ray crystallographic structure of rabbit PrP has identified a key helix-capping motif implicated in the low prion disease susceptibility of rabbits. Removal of this capping motif increases the beta-structure folding propensity of rabbit PrP to match that of PrP from mouse, a species more susceptible to prion disease.

Prion disease susceptibility is affected by {beta}-structure folding propensity and local side-chain interactions in PrP.,Khan MQ, Sweeting B, Mulligan VK, Arslan PE, Cashman NR, Pai EF, Chakrabartty A Proc Natl Acad Sci U S A. 2010 Nov 16;107(46):19808-19813. Epub 2010 Nov, 1. PMID:21041683[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Khan MQ, Sweeting B, Mulligan VK, Arslan PE, Cashman NR, Pai EF, Chakrabartty A. Prion disease susceptibility is affected by {beta}-structure folding propensity and local side-chain interactions in PrP. Proc Natl Acad Sci U S A. 2010 Nov 16;107(46):19808-19813. Epub 2010 Nov, 1. PMID:21041683 doi:10.1073/pnas.1005267107

3o79, resolution 1.60Å

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