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1uw3

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[[Image:1uw3.jpg|left|200px]]
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{{STRUCTURE_1uw3| PDB=1uw3 | SCENE= }}
{{STRUCTURE_1uw3| PDB=1uw3 | SCENE= }}
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'''THE CRYSTAL STRUCTURE OF THE GLOBULAR DOMAIN OF SHEEP PRION PROTEIN'''
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===THE CRYSTAL STRUCTURE OF THE GLOBULAR DOMAIN OF SHEEP PRION PROTEIN===
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==Overview==
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The prion protein PrP is a naturally occurring polypeptide that becomes transformed from a normal conformation to that of an aggregated form, characteristic of pathological states in fatal transmissible spongiform conditions such as Creutzfeld-Jacob Disease and Bovine Spongiform Encephalopathy. We report the crystal structure, at 2 A resolution, of residues 123-230 of the C-terminal globular domain of the ARQ allele of sheep prion protein (PrP). The asymmetric unit contains a single molecule whose secondary structure and overall organisation correspond to those structures of PrPs from various mammalian species determined by NMR. The globular domain shows a close association of helix-1, the C-terminal portion of helix-2 and the N-terminal portion of helix-3, bounded by the intramolecular disulphide bond, 179-214. The loop 164-177, between beta2 and helix-2 is relatively well structured compared to the human PrP NMR structure. Analysis of the sheep PrP structure identifies two possible loci for the initiation of beta-sheet mediated polymerisation. One of these comprises the beta-strand, residues 129-131 that forms an intra-molecular beta-sheet with residues 161-163. This strand is involved in lattice contacts about a crystal dyad to generate a four-stranded intermolecular beta-sheet between neighbouring molecules. The second locus involves the region 188-204, which modelling suggests is able to undergo a partial alpha--&gt;beta switch within the monomer. These loci provide sites within the PrPc monomer that could readily give rise to early intermediate species on the pathway to the formation of aggregated PrPSc containing additional intermolecular beta-structure.
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The line below this paragraph, {{ABSTRACT_PUBMED_15037077}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 15037077 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15037077}}
==About this Structure==
==About this Structure==
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[[Category: Sheep]]
[[Category: Sheep]]
[[Category: Transmissible spongiform encephalopathy]]
[[Category: Transmissible spongiform encephalopathy]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:45:39 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:41:51 2008''

Revision as of 04:41, 28 July 2008

Image:1uw3.png

Template:STRUCTURE 1uw3

THE CRYSTAL STRUCTURE OF THE GLOBULAR DOMAIN OF SHEEP PRION PROTEIN

Template:ABSTRACT PUBMED 15037077

About this Structure

1UW3 is a Single protein structure of sequence from Ovis aries. Full crystallographic information is available from OCA.

Reference

The crystal structure of the globular domain of sheep prion protein., Haire LF, Whyte SM, Vasisht N, Gill AC, Verma C, Dodson EJ, Dodson GG, Bayley PM, J Mol Biol. 2004 Mar 5;336(5):1175-83. PMID:15037077

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