2fj3

From Proteopedia

(Difference between revisions)

Revision as of 08:51, 16 January 2015

NMR solution of rabbit Prion Protein (91-228)

Structural highlights

2fj3 is a 1 chain structure with sequence from Oryctolagus cuniculus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, RCSB, PDBsum

Disease

[PRIO_RABIT] Note=Found in high quantity in the brain of humans and animals infected with degenerative neurological diseases such as kuru, Creutzfeldt-Jakob disease (CJD), Gerstmann-Straussler syndrome (GSS), scrapie, bovine spongiform encephalopathy (BSE), transmissible mink encephalopathy (TME), etc.

Function

[PRIO_RABIT] 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.

Publication Abstract from PubMed

Rabbits are one of the few mammalian species that appear to be resistant to transmissible spongiform encephalopathies due to the structural characteristics of the rabbit prion protein (RaPrPC) itself. Here we determined the solution structures of the recombinant protein RaPrPC-(91-228) and its S173N variant, and detected the backbone dynamics of their structured C-terminal domains-(121-228). In contrast to many other mammalian PrPCs, loop 165-172 that connects beta-sheet-2 and alpha-helix-2 is well-defined in RaPrPC. For the first time, order parameters S2 were obtained for residues in this loop region, indicating that loop 165-172 of RaPrPC is highly ordered. Compared with the wild-type RaPrPC, less hydrogen bonds form in the S173N variant. The NMR dynamics analysis reveals a distinct increase in the structural flexibility of loop 165-172 and helix-3 after the S173N substitution, implying that the S173N substitution disturbs the long-range interaction of loop 165-172 with helix-3, which further leads to a marked decrease in the global conformational stability. Significantly, RaPrPC possesses a unique charge distribution, carrying a continuous area of positive charges on the surface, which is distinguished from other PrPCs. The S173N substitution causes visible changes of the charge distribution around the recognition sites for the hypothetical protein X. Our results suggest that the ordered loop 165-172 and its interaction with helix-3, together with the unique distribution of surface electrostatic potential, significantly contribute to the unique structural characteristics of RaPrPC.

Unique structural characteristics of the rabbit prion protein.,Wen Y, Li J, Yao W, Xiong M, Hong J, Peng Y, Xiao G, Lin D J Biol Chem. 2010 Jul 16. PMID:20639199^[1]

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

References

↑ Wen Y, Li J, Yao W, Xiong M, Hong J, Peng Y, Xiao G, Lin D. Unique structural characteristics of the rabbit prion protein. J Biol Chem. 2010 Jul 16. PMID:20639199 doi:10.1074/jbc.M110.118844

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/2fj3"

Categories: Oryctolagus cuniculus | Li, J | Lin, D H | Membrane protein | Prion protein

@@ Line 3: / Line 3: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[2fj3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FJ3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FJ3 FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fj3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fj3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2fj3 RCSB], [http://www.ebi.ac.uk/pdbsum/2fj3 PDBsum]</span></td></tr>
+</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fj3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fj3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2fj3 RCSB], [http://www.ebi.ac.uk/pdbsum/2fj3 PDBsum]</span></td></tr>
-<table>
+</table>
 == Disease ==
 [[http://www.uniprot.org/uniprot/PRIO_RABIT PRIO_RABIT]] Note=Found in high quantity in the brain of humans and animals infected with degenerative neurological diseases such as kuru, Creutzfeldt-Jakob disease (CJD), Gerstmann-Straussler syndrome (GSS), scrapie, bovine spongiform encephalopathy (BSE), transmissible mink encephalopathy (TME), etc.
@@ Line 35: / Line 35: @@
 </StructureSection>
 [[Category: Oryctolagus cuniculus]]
-[[Category: Li, J.]]
+[[Category: Li, J]]
-[[Category: Lin, D H.]]
+[[Category: Lin, D H]]
 [[Category: Membrane protein]]
 [[Category: Prion protein]]

2fj3

From Proteopedia

Revision as of 08:51, 16 January 2015

NMR solution of rabbit Prion Protein (91-228)

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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