View source for 1dx1


==BOVINE PRION PROTEIN RESIDUES 23-230==
<StructureSection load='1dx1' size='340' side='right'caption='[[1dx1]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1dx1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DX1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DX1 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=1dx1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dx1 OCA], [https://pdbe.org/1dx1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dx1 RCSB], [https://www.ebi.ac.uk/pdbsum/1dx1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dx1 ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/PRIO_BOVIN PRIO_BOVIN] Note=Variations in PRNP are responsible of transmissible bovine spongiform encephalopathies (BSE), a class of neurodegenerative diseases that affect various mammals. These diseases are caused by abnormally folded prion proteins. BSE can be subdivided into at least three groups: classical, H-type and L-type, with the latter 2 collectively referred to as atypical BSE. Susceptibility or resistance to a BSE disease can be influenced by at least 3 factors related to the host prion protein: protein expression levels, number of octapeptide repeats, and specific polymorphisms. In cattle, as in humans, BSEs can occur as infectious, spontaneous and genetic diseases.
== Function ==
[https://www.uniprot.org/uniprot/PRIO_BOVIN PRIO_BOVIN] May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May play a role in iron uptake and iron homeostasis. Soluble oligomers are toxic to cultured neuroblastoma cells and induce apoptosis (in vitro). Association with GPC1 (via its heparan sulfate chains) targets PRNP to lipid rafts. Also provides Cu(2+) or ZN(2+) for the ascorbate-mediated GPC1 deaminase degradation of its heparan sulfate side chains (By similarity).
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dx/1dx1_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1dx1 ConSurf].
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== Publication Abstract from PubMed ==
The NMR structures of the recombinant 217-residue polypeptide chain of the mature bovine prion protein, bPrP(23-230), and a C-terminal fragment, bPrP(121-230), include a globular domain extending from residue 125 to residue 227, a short flexible chain end of residues 228-230, and an N-terminal flexibly disordered "tail" comprising 108 residues for the intact protein and 4 residues for bPrP(121-230), respectively. The globular domain contains three alpha-helices comprising the residues 144-154, 173-194, and 200-226, and a short antiparallel beta-sheet comprising the residues 128-131 and 161-164. The best-defined parts of the globular domain are the central portions of the helices 2 and 3, which are linked by the only disulfide bond in bPrP. Significantly increased disorder and mobility is observed for helix 1, the loop 166-172 leading from the beta-strand 2 to helix 2, the end of helix 2 and the following loop, and the last turn of helix 3. Although there are characteristic local differences relative to the conformations of the murine and Syrian hamster prion proteins, the bPrP structure is essentially identical to that of the human prion protein. On the other hand, there are differences between bovine and human PrP in the surface distribution of electrostatic charges, which then appears to be the principal structural feature of the "healthy" PrP form that might affect the stringency of the species barrier for transmission of prion diseases between humans and cattle.

NMR structure of the bovine prion protein.,Lopez Garcia F, Zahn R, Riek R, Wuthrich K Proc Natl Acad Sci U S A. 2000 Jul 18;97(15):8334-9. PMID:10899999<ref>PMID:10899999</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
*[[Prion 3D structures|Prion 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bos taurus]]
[[Category: Large Structures]]
[[Category: Billeter M]]
[[Category: Lopez Garcia F]]
[[Category: Riek R]]
[[Category: Wuthrich K]]
[[Category: Zahn R]]