1xyk

From Proteopedia

(Difference between revisions)

Current revision

NMR Structure of the canine prion protein

Structural highlights

1xyk is a 1 chain structure with sequence from Canis lupus familiaris. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

PRIO_CANLF PrP is found in high quantity in the brain of humans and animals infected with the degenerative neurological diseases kuru, Creutzfeldt-Jakob disease (CJD), Gerstmann-Straussler syndrome (GSS), scrapie, bovine spongiform encephalopathy (BSE), transmissible mink encephalopathy (TME), etc.

Function

PRIO_CANLF Its primary physiological function is unclear. May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May promote myelin homeostasis through acting as an agonist for ADGRG6 receptor. May play a role in iron uptake and iron homeostasis. Soluble oligomers are toxic to cultured neuroblastoma cells and induce apoptosis (in vitro) (By similarity). 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).[UniProtKB:P04156][UniProtKB:P04925]

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 cellular form of the prion proteins (PrPC) of the cat (Felis catus), dog (Canis familiaris), and pig (Sus scrofa), and of two polymorphic forms of the prion protein from sheep (Ovis aries) are presented. In all of these species, PrPC consists of an N-terminal flexibly extended tail with approximately 100 amino acid residues and a C-terminal globular domain of approximately 100 residues with three alpha-helices and a short antiparallel beta-sheet. Although this global architecture coincides with the previously reported murine, Syrian hamster, bovine, and human PrPC structures, there are local differences between the globular domains of the different species. Because the five newly determined PrPC structures originate from species with widely different transmissible spongiform encephalopathy records, the present data indicate previously uncharacterized possible correlations between local features in PrPC three-dimensional structures and susceptibility of different mammalian species to transmissible spongiform encephalopathies.

Prion protein NMR structures of cats, dogs, pigs, and sheep.,Lysek DA, Schorn C, Nivon LG, Esteve-Moya V, Christen B, Calzolai L, von Schroetter C, Fiorito F, Herrmann T, Guntert P, Wuthrich K Proc Natl Acad Sci U S A. 2005 Jan 18;102(3):640-5. Epub 2005 Jan 12. PMID:15647367^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Lysek DA, Schorn C, Nivon LG, Esteve-Moya V, Christen B, Calzolai L, von Schroetter C, Fiorito F, Herrmann T, Guntert P, Wuthrich K. Prion protein NMR structures of cats, dogs, pigs, and sheep. Proc Natl Acad Sci U S A. 2005 Jan 18;102(3):640-5. Epub 2005 Jan 12. PMID:15647367

1 Structural highlights
2 Disease
3 Function
4 Evolutionary Conservation
5 Publication Abstract from PubMed
6 See Also
7 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1xyk"

@@ Line 1: / Line 1: @@
 ==NMR Structure of the canine prion protein==
-<StructureSection load='1xyk' size='340' side='right'caption='[[1xyk]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='1xyk' size='340' side='right'caption='[[1xyk]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1xyk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Canlf Canlf]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XYK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XYK FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1xyk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Canis_lupus_familiaris Canis lupus familiaris]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XYK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XYK 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;'>[[1xyj|1xyj]], [[1xyq|1xyq]]</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xyk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xyk OCA], [https://pdbe.org/1xyk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xyk RCSB], [https://www.ebi.ac.uk/pdbsum/1xyk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xyk ProSAT]</span></td></tr>
 </table>
 == Disease ==
-[[https://www.uniprot.org/uniprot/PRIO_CANFA PRIO_CANFA]] Note=PrP is found in high quantity in the brain of humans and animals infected with the degenerative neurological diseases kuru, Creutzfeldt-Jakob disease (CJD), Gerstmann-Straussler syndrome (GSS), scrapie, bovine spongiform encephalopathy (BSE), transmissible mink encephalopathy (TME), etc.
+[https://www.uniprot.org/uniprot/PRIO_CANLF PRIO_CANLF] PrP is found in high quantity in the brain of humans and animals infected with the degenerative neurological diseases kuru, Creutzfeldt-Jakob disease (CJD), Gerstmann-Straussler syndrome (GSS), scrapie, bovine spongiform encephalopathy (BSE), transmissible mink encephalopathy (TME), etc.
 == Function ==
-[[https://www.uniprot.org/uniprot/PRIO_CANFA PRIO_CANFA]] 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).
+[https://www.uniprot.org/uniprot/PRIO_CANLF PRIO_CANLF] Its primary physiological function is unclear. May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May promote myelin homeostasis through acting as an agonist for ADGRG6 receptor. May play a role in iron uptake and iron homeostasis. Soluble oligomers are toxic to cultured neuroblastoma cells and induce apoptosis (in vitro) (By similarity). 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).[UniProtKB:P04156][UniProtKB:P04925]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 37: / Line 37: @@
 __TOC__
 </StructureSection>
-[[Category: Canlf]]
+[[Category: Canis lupus familiaris]]
 [[Category: Large Structures]]
-[[Category: Esteve-Moya, V]]
+[[Category: Esteve-Moya V]]
-[[Category: Herrmann, T]]
+[[Category: Herrmann T]]
-[[Category: Lysek, D A]]
+[[Category: Lysek DA]]
-[[Category: Schorn, C]]
+[[Category: Schorn C]]
-[[Category: Wuthrich, K]]
+[[Category: Wuthrich K]]
-[[Category: Cprp]]
-[[Category: Prion]]
-[[Category: Prnp]]
-[[Category: Prp]]
-[[Category: Unknown function]]

1xyk

From Proteopedia

Current revision

NMR Structure of the canine prion protein

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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