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| | ==Horse prion protein== | | ==Horse prion protein== |
| - | <StructureSection load='2ku4' size='340' side='right' caption='[[2ku4]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2ku4' size='340' side='right'caption='[[2ku4]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2ku4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KU4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KU4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2ku4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KU4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KU4 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ku5|2ku5]], [[2ku6|2ku6]]</td></tr> | + | </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=2ku4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ku4 OCA], [https://pdbe.org/2ku4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ku4 RCSB], [https://www.ebi.ac.uk/pdbsum/2ku4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ku4 ProSAT]</span></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=9796 Equus caballus])</td></tr>
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| - | <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=2ku4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ku4 OCA], [http://pdbe.org/2ku4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ku4 RCSB], [http://www.ebi.ac.uk/pdbsum/2ku4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ku4 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/O97964_HORSE O97964_HORSE] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Prion|Prion]] | + | *[[Prion 3D structures|Prion 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Equus caballus]] | | [[Category: Equus caballus]] |
| - | [[Category: Damberger, F F]] | + | [[Category: Large Structures]] |
| - | [[Category: Perez, D R]] | + | [[Category: Damberger FF]] |
| - | [[Category: Wuthrich, K]] | + | [[Category: Perez DR]] |
| - | [[Category: Amyloid]] | + | [[Category: Wuthrich K]] |
| - | [[Category: Cell membrane]]
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| - | [[Category: Ecprp]]
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| - | [[Category: Horse]]
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| - | [[Category: Membrane]]
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| - | [[Category: Membrane protein]]
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| - | [[Category: Prion]]
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| Structural highlights
Function
O97964_HORSE
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 NMR structure of the horse (Equus caballus) cellular prion protein at 25 degrees C exhibits the typical PrP(C) [cellular form of prion protein (PrP)] global architecture, but in contrast to most other mammalian PrP(C)s, it contains a well-structured loop connecting the beta2 strand with the alpha2 helix. Comparison with designed variants of the mouse prion protein resulted in the identification of a single amino acid exchange within the loop, D167S, which correlates with the high structural order of this loop in the solution structure at 25 degrees C and is unique to the PrP sequences of equine species. The beta2-alpha2 loop and the alpha3 helix form a protein surface epitope that has been proposed to be the recognition area for a hypothetical chaperone, "protein X," which would promote conversion of PrP(C) into the disease-related scrapie form and thus mediate intermolecular interactions related to the transmission barrier for transmissible spongiform encephalopathies (TSEs) between different species. The present results are evaluated in light of recent indications from in vivo experiments that the local beta2-alpha2 loop structure affects the susceptibility of transgenic mice to TSEs and the fact that there are no reports on TSE in horses.
Horse prion protein NMR structure and comparisons with related variants of the mouse prion protein.,Perez DR, Damberger FF, Wuthrich K J Mol Biol. 2010 Jul 9;400(2):121-8. Epub 2010 May 8. PMID:20460128[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Perez DR, Damberger FF, Wuthrich K. Horse prion protein NMR structure and comparisons with related variants of the mouse prion protein. J Mol Biol. 2010 Jul 9;400(2):121-8. Epub 2010 May 8. PMID:20460128 doi:10.1016/j.jmb.2010.04.066
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