1qm0

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(New page: 200px<br /> <applet load="1qm0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qm0" /> '''HUMAN PRION PROTEIN FRAGMENT 90-230'''<br /...)
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'''HUMAN PRION PROTEIN FRAGMENT 90-230'''<br />
'''HUMAN PRION PROTEIN FRAGMENT 90-230'''<br />
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==About this Structure==
==About this Structure==
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1QM0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QM0 OCA].
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1QM0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QM0 OCA].
==Reference==
==Reference==
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[[Category: repeat]]
[[Category: repeat]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:54:33 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:45:09 2008''

Revision as of 14:45, 15 February 2008


1qm0

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HUMAN PRION PROTEIN FRAGMENT 90-230

Contents

Overview

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.

Disease

Known diseases 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], Retinitis pigmentosa-11 OMIM:[606419]

About this Structure

1QM0 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

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

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