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==BOVINE PRION PROTEIN RESIDUES 23-230== | ==BOVINE PRION PROTEIN RESIDUES 23-230== | ||
<StructureSection load='1dx1' size='340' side='right'caption='[[1dx1 | <StructureSection load='1dx1' size='340' side='right'caption='[[1dx1]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1dx1]] is a 1 chain structure with sequence from [ | <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=' | </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='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> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Disease == | == 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 == | == 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 22: | Line 21: | ||
</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]. | </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]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
==See Also== | ==See Also== | ||
*[[Prion 3D structures|Prion 3D structures]] | *[[Prion 3D structures|Prion 3D structures]] | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Bos taurus]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Billeter | [[Category: Billeter M]] | ||
[[Category: Garcia | [[Category: Lopez Garcia F]] | ||
[[Category: Riek | [[Category: Riek R]] | ||
[[Category: Wuthrich | [[Category: Wuthrich K]] | ||
[[Category: Zahn | [[Category: Zahn R]] | ||
Revision as of 12:55, 20 March 2024
BOVINE PRION PROTEIN RESIDUES 23-230BOVINE PRION PROTEIN RESIDUES 23-230
Structural highlights
DiseasePRIO_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. FunctionPRIO_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 Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See Also |
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