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| | ==Solution structure of Xenopus leavis prion protein== | | ==Solution structure of Xenopus leavis prion protein== |
| - | <StructureSection load='1xu0' size='340' side='right'caption='[[1xu0]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='1xu0' size='340' side='right'caption='[[1xu0]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1xu0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/African_clawed_frog African clawed frog]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XU0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XU0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1xu0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XU0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XU0 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1u3m|1u3m]], [[1u5l|1u5l]]</div></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">prnp ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8355 African clawed frog])</td></tr>
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| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xu0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xu0 OCA], [https://pdbe.org/1xu0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xu0 RCSB], [https://www.ebi.ac.uk/pdbsum/1xu0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xu0 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=1xu0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xu0 OCA], [https://pdbe.org/1xu0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xu0 RCSB], [https://www.ebi.ac.uk/pdbsum/1xu0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xu0 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q5S1W7_XENLA Q5S1W7_XENLA] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: African clawed frog]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Perez, D R]] | + | [[Category: Xenopus laevis]] |
| - | [[Category: Wuthrich, K]] | + | [[Category: Perez DR]] |
| - | [[Category: Amphibian]] | + | [[Category: Wuthrich K]] |
| - | [[Category: Glycoprotein]]
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| - | [[Category: Membrane protein]]
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| - | [[Category: Polymorphism]]
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| - | [[Category: Prion]]
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| Structural highlights
Function
Q5S1W7_XENLA
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 structures of the recombinant prion proteins from chicken (Gallus gallus; chPrP), the red-eared slider turtle (Trachemys scripta; tPrP), and the African clawed frog (Xenopus laevis; xlPrP) are presented. The amino acid sequences of these prion proteins show approximately 30% identity with mammalian prion proteins. All three species form the same molecular architecture as mammalian PrPC, with a long, flexibly disordered tail attached to the N-terminal end of a globular domain. The globular domain in chPrP and tPrP contains three alpha-helices, one short 3(10)-helix, and a short antiparallel beta-sheet. In xlPrP, the globular domain includes three alpha-helices and a somewhat longer beta-sheet than in the other species. The spatial arrangement of these regular secondary structures coincides closely with that of the globular domain in mammalian prion proteins. Based on the low sequence identity to mammalian PrPs, comparison of chPrP, tPrP, and xlPrP with mammalian PrPC structures is used to identify a set of essential amino acid positions for the preservation of the same PrPC fold in birds, reptiles, amphibians, and mammals. There are additional conserved residues without apparent structural roles, which are of interest for the ongoing search for physiological functions of PrPC in healthy organisms.
Prion protein NMR structures of chickens, turtles, and frogs.,Calzolai L, Lysek DA, Perez DR, Guntert P, Wuthrich K Proc Natl Acad Sci U S A. 2005 Jan 18;102(3):651-5. Epub 2005 Jan 12. PMID:15647366[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Calzolai L, Lysek DA, Perez DR, Guntert P, Wuthrich K. Prion protein NMR structures of chickens, turtles, and frogs. Proc Natl Acad Sci U S A. 2005 Jan 18;102(3):651-5. Epub 2005 Jan 12. PMID:15647366
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