View source for 2l1d


==Mouse prion protein (121-231) containing the substitution Y169G==
<StructureSection load='2l1d' size='340' side='right'caption='[[2l1d]]' scene=''>
== Structural highlights ==
<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='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'>[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>
</table>
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== 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<ref>PMID:21987789</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2l1d" style="background-color:#fffaf0;"></div>

==See Also==
*[[Prion 3D structures|Prion 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Christen B]]
[[Category: Damberger FF]]
[[Category: Hornemann S]]
[[Category: Perez DR]]
[[Category: Wuthrich K]]