3fva

From Proteopedia

(Difference between revisions)

Revision as of 09:33, 6 December 2023

NNQNTF segment from elk prion

Structural highlights

3fva is a 1 chain structure with sequence from Cervus canadensis nelsoni. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.458Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

PRIO_CEREN 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.

Function

PRIO_CEREN 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).

Publication Abstract from PubMed

In prion inheritance and transmission, strains are phenotypic variants encoded by protein 'conformations'. However, it is unclear how a protein conformation can be stable enough to endure transmission between cells or organisms. Here we describe new polymorphic crystal structures of segments of prion and other amyloid proteins, which offer two structural mechanisms for the encoding of prion strains. In packing polymorphism, prion strains are encoded by alternative packing arrangements (polymorphs) of beta-sheets formed by the same segment of a protein; in segmental polymorphism, prion strains are encoded by distinct beta-sheets built from different segments of a protein. Both forms of polymorphism can produce enduring conformations capable of encoding strains. These molecular mechanisms for transfer of protein-encoded information into prion strains share features with the familiar mechanism for transfer of nucleic acid-encoded information into microbial strains, including sequence specificity and recognition by noncovalent bonds.

Molecular mechanisms for protein-encoded inheritance.,Wiltzius JJ, Landau M, Nelson R, Sawaya MR, Apostol MI, Goldschmidt L, Soriaga AB, Cascio D, Rajashankar K, Eisenberg D Nat Struct Mol Biol. 2009 Sep;16(9):973-8. Epub 2009 Aug 16. PMID:19684598^[1]

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

References

↑ Wiltzius JJ, Landau M, Nelson R, Sawaya MR, Apostol MI, Goldschmidt L, Soriaga AB, Cascio D, Rajashankar K, Eisenberg D. Molecular mechanisms for protein-encoded inheritance. Nat Struct Mol Biol. 2009 Sep;16(9):973-8. Epub 2009 Aug 16. PMID:19684598 doi:10.1038/nsmb.1643

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3fva"

Categories: Cervus canadensis nelsoni | Large Structures | Apostol MI | Eisenberg D

@@ Line 3: / Line 3: @@
 <StructureSection load='3fva' size='340' side='right'caption='[[3fva]], [[Resolution|resolution]] 1.46&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3fva]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FVA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FVA FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3fva]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cervus_canadensis_nelsoni Cervus canadensis nelsoni]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FVA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FVA FirstGlance]. <br>
-</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=3fva FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fva OCA], [https://pdbe.org/3fva PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fva RCSB], [https://www.ebi.ac.uk/pdbsum/3fva PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fva ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.458&#8491;</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=3fva FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fva OCA], [https://pdbe.org/3fva PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fva RCSB], [https://www.ebi.ac.uk/pdbsum/3fva PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fva ProSAT]</span></td></tr>
 </table>
 == Disease ==
-[[https://www.uniprot.org/uniprot/PRIO_CEREN PRIO_CEREN]] 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_CEREN PRIO_CEREN] 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.
 == Function ==
-[[https://www.uniprot.org/uniprot/PRIO_CEREN PRIO_CEREN]] 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_CEREN PRIO_CEREN] 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).
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 26: / Line 27: @@
 __TOC__
 </StructureSection>
+[[Category: Cervus canadensis nelsoni]]
 [[Category: Large Structures]]
-[[Category: Apostol, M I]]
+[[Category: Apostol MI]]
-[[Category: Eisenberg, D]]
+[[Category: Eisenberg D]]
-[[Category: Amyloid-like protofibril]]
-[[Category: Cell membrane]]
-[[Category: Glycoprotein]]
-[[Category: Golgi apparatus]]
-[[Category: Gpi-anchor]]
-[[Category: Lipoprotein]]
-[[Category: Membrane]]
-[[Category: Prion]]
-[[Category: Protein fibril]]

3fva

From Proteopedia

Revision as of 09:33, 6 December 2023

NNQNTF segment from elk prion

Structural highlights

Disease

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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