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| | ==Mouse prion protein (121-231) containing the substitution Y169G== | | ==Mouse prion protein (121-231) containing the substitution Y169G== |
| - | <StructureSection load='2l1d' size='340' side='right' caption='[[2l1d]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2l1d' size='340' side='right'caption='[[2l1d]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2l1d]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L1D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2L1D FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2l1d]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L1D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L1D FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2l1e|2l1e]], [[2l1h|2l1h]], [[2l1k|2l1k]]</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Prnp, RP23-401J24.1-001 ([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'>[https://proteopedia.org/fgij/fg.htm?mol=2l1d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l1d OCA], [https://pdbe.org/2l1d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l1d RCSB], [https://www.ebi.ac.uk/pdbsum/2l1d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l1d ProSAT]</span></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=2l1d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l1d OCA], [http://pdbe.org/2l1d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2l1d RCSB], [http://www.ebi.ac.uk/pdbsum/2l1d PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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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: Lk3 transgenic mice]] | + | [[Category: Large Structures]] |
| - | [[Category: Christen, B]] | + | [[Category: Mus musculus]] |
| - | [[Category: Damberger, F F]] | + | [[Category: Christen B]] |
| - | [[Category: Hornemann, S]] | + | [[Category: Damberger FF]] |
| - | [[Category: Perez, D R]] | + | [[Category: Hornemann S]] |
| - | [[Category: Wuthrich, K]] | + | [[Category: Perez DR]] |
| - | [[Category: Membrane protein]]
| + | [[Category: Wuthrich K]] |
| - | [[Category: Mutation]]
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| - | [[Category: Prion]]
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| Structural highlights
Publication Abstract from PubMed
In the otherwise highly conserved NMR structures of cellular prion proteins (PrP(C)) from different mammals, species variations in a surface epitope that includes a loop linking a beta-strand, beta2, with a helix, alpha2, are associated with NMR manifestations of a dynamic equilibrium between locally different conformations. Here, it is shown that this local dynamic conformational polymorphism in mouse PrP(C) is eliminated through exchange of Tyr169 by Ala or Gly, but is preserved after exchange of Tyr 169 with Phe. NMR structure determinations of designed variants of mouse PrP(121-231) at 20 degrees C and of wild-type mPrP(121-231) at 37 degrees C together with analysis of exchange effects on NMR signals then resulted in the identification of the two limiting structures involved in this local conformational exchange in wild-type mouse PrP(C), and showed that the two exchanging structures present characteristically different solvent-exposed epitopes near the beta2-alpha2 loop. The structural data presented in this paper provided a platform for currently ongoing, rationally designed experiments with transgenic laboratory animals for renewed attempts to unravel the so far elusive physiological function of the cellular prion protein.
Cellular prion protein conformation and function.,Damberger FF, Christen B, Perez DR, Hornemann S, Wuthrich K Proc Natl Acad Sci U S A. 2011 Oct 18;108(42):17308-13. Epub 2011 Oct 10. PMID:21987789[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Damberger FF, Christen B, Perez DR, Hornemann S, Wuthrich K. Cellular prion protein conformation and function. Proc Natl Acad Sci U S A. 2011 Oct 18;108(42):17308-13. Epub 2011 Oct 10. PMID:21987789 doi:10.1073/pnas.1106325108
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