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| ==Bank Vole Prion Protein (121-231)== | | ==Bank Vole Prion Protein (121-231)== |
- | <StructureSection load='2k56' size='340' side='right' caption='[[2k56]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2k56' size='340' side='right'caption='[[2k56]]' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[2k56]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bank_vole Bank vole]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K56 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2K56 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2k56]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Myodes_glareolus Myodes glareolus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K56 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2K56 FirstGlance]. <br> |
- | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PrP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=447135 Bank vole])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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=2k56 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k56 OCA], [http://pdbe.org/2k56 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2k56 RCSB], [http://www.ebi.ac.uk/pdbsum/2k56 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2k56 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=2k56 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k56 OCA], [https://pdbe.org/2k56 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k56 RCSB], [https://www.ebi.ac.uk/pdbsum/2k56 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k56 ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Evolutionary Conservation == | | == Evolutionary Conservation == |
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| <jmolCheckbox> | | <jmolCheckbox> |
| <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k5/2k56_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k5/2k56_consurf.spt"</scriptWhenChecked> |
- | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| </jmolCheckbox> | | </jmolCheckbox> |
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| ==See Also== | | ==See Also== |
- | *[[Prion|Prion]] | + | *[[Prion 3D structures|Prion 3D structures]] |
| == References == | | == References == |
| <references/> | | <references/> |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Bank vole]] | + | [[Category: Large Structures]] |
- | [[Category: Christen, B]] | + | [[Category: Myodes glareolus]] |
- | [[Category: Hornemann, S]] | + | [[Category: Christen B]] |
- | [[Category: Wuthrich, K]] | + | [[Category: Hornemann S]] |
- | [[Category: Membrane]] | + | [[Category: Wuthrich K]] |
- | [[Category: Prion protein]]
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- | [[Category: Unknown function]]
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| Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The recent introduction of bank vole (Clethrionomys glareolus) as an additional laboratory animal for research on prion diseases revealed an important difference when compared to the mouse and the Syrian hamster, since bank voles show a high susceptibility to infection by brain homogenates from a wide range of diseased species such as sheep, goats, and humans. In this context, we determined the NMR structure of the C-terminal globular domain of the recombinant bank vole prion protein (bvPrP) [bvPrP(121-231)] at 20 degrees C. bvPrP(121-231) has the same overall architecture as other mammalian PrPs, with three alpha-helices and an antiparallel beta-sheet, but it differs from PrP of the mouse and most other mammalian species in that the loop connecting the second beta-strand and helix alpha2 is precisely defined at 20 degrees C. This is similar to the previously described structures of elk PrP and the designed mouse PrP (mPrP) variant mPrP[S170N,N174T](121-231), whereas Syrian hamster PrP displays a structure that is in-between these limiting cases. Studies with the newly designed variant mPrP[S170N](121-231), which contains the same loop sequence as bvPrP, now also showed that the single-amino-acid substitution S170N in mPrP is sufficient for obtaining a well-defined loop, thus providing the rationale for this local structural feature in bvPrP.
NMR structure of the bank vole prion protein at 20 degrees C contains a structured loop of residues 165-171.,Christen B, Perez DR, Hornemann S, Wuthrich K J Mol Biol. 2008 Nov 7;383(2):306-12. Epub 2008 Aug 26. PMID:18773909[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Christen B, Perez DR, Hornemann S, Wuthrich K. NMR structure of the bank vole prion protein at 20 degrees C contains a structured loop of residues 165-171. J Mol Biol. 2008 Nov 7;383(2):306-12. Epub 2008 Aug 26. PMID:18773909 doi:10.1016/j.jmb.2008.08.045
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