1qlz: Difference between revisions
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'''HUMAN PRION PROTEIN''' | '''HUMAN PRION PROTEIN''' | ||
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[[Category: Wuthrich, K.]] | [[Category: Wuthrich, K.]] | ||
[[Category: Zahn, R.]] | [[Category: Zahn, R.]] | ||
[[Category: | [[Category: Brain]] | ||
[[Category: | [[Category: Disease mutation]] | ||
[[Category: | [[Category: Glycoprotein]] | ||
[[Category: | [[Category: Gpi-anchor]] | ||
[[Category: | [[Category: Polymorphism]] | ||
[[Category: | [[Category: Prion]] | ||
[[Category: | [[Category: Repeat]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:25:59 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 06:26, 3 May 2008
HUMAN PRION PROTEIN
OverviewOverview
The NMR structures of the recombinant human prion protein, hPrP(23-230), and two C-terminal fragments, hPrP(90-230) and hPrP(121-230), include a globular domain extending from residues 125-228, for which a detailed structure was obtained, and an N-terminal flexibly disordered "tail." The globular domain contains three alpha-helices comprising the residues 144-154, 173-194, and 200-228 and a short anti-parallel beta-sheet comprising the residues 128-131 and 161-164. Within the globular domain, three polypeptide segments show increased structural disorder: i.e., a loop of residues 167-171, the residues 187-194 at the end of helix 2, and the residues 219-228 in the C-terminal part of helix 3. The local conformational state of the polypeptide segments 187-193 in helix 2 and 219-226 in helix 3 is measurably influenced by the length of the N-terminal tail, with the helical states being most highly populated in hPrP(23-230). When compared with the previously reported structures of the murine and Syrian hamster prion proteins, the length of helix 3 coincides more closely with that in the Syrian hamster protein whereas the disordered loop 167-171 is shared with murine PrP. These species variations of local structure are in a surface area of the cellular form of PrP that has previously been implicated in intermolecular interactions related both to the species barrier for infectious transmission of prion disease and to immune reactions.
DiseaseDisease
Known disease associated with this structure: Creutzfeldt-Jakob disease OMIM:[176640], Gerstmann-Straussler disease OMIM:[176640], Huntington disease-like 1 OMIM:[176640], Insomnia, fatal familial OMIM:[176640], Prion disease with protracted course OMIM:[176640]
About this StructureAbout this Structure
1QLZ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
NMR solution structure of the human prion protein., Zahn R, Liu A, Luhrs T, Riek R, von Schroetter C, Lopez Garcia F, Billeter M, Calzolai L, Wider G, Wuthrich K, Proc Natl Acad Sci U S A. 2000 Jan 4;97(1):145-50. PMID:10618385 Page seeded by OCA on Sat May 3 06:25:59 2008