1h0l
From Proteopedia
(New page: 200px<br /> <applet load="1h0l" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h0l" /> '''HUMAN PRION PROTEIN 121-230 M166C/E221C'''<...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1h0l. | + | [[Image:1h0l.jpg|left|200px]]<br /><applet load="1h0l" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1h0l" size=" | + | |
caption="1h0l" /> | caption="1h0l" /> | ||
'''HUMAN PRION PROTEIN 121-230 M166C/E221C'''<br /> | '''HUMAN PRION PROTEIN 121-230 M166C/E221C'''<br /> | ||
| Line 11: | Line 10: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1H0L 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:// | + | 1H0L 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=1H0L OCA]. |
==Reference== | ==Reference== | ||
| Line 30: | Line 29: | ||
[[Category: repeat]] | [[Category: repeat]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:55:05 2008'' |
Revision as of 13:55, 15 February 2008
|
HUMAN PRION PROTEIN 121-230 M166C/E221C
Contents |
Overview
The nuclear magnetic resonance structure of the globular domain with, residues 121-230 of a variant human prion protein with two disulfide, bonds, hPrP(M166C/E221C), shows the same global fold as wild-type, hPrP(121-230). It contains three alpha-helices of residues 144-154, 173-194 and 200-228, an anti-parallel beta-sheet of residues 128-131 and, 161-164, and the disulfides Cys166-Cys221 and Cys179-Cys214. The, engineered extra disulfide bond in the presumed "protein X"-binding site, is accommodated with slight, strictly localized conformational changes., High compatibility of hPrP with insertion of a second disulfide bridge in, the protein X epitope was further substantiated by model calculations with, additional variant structures. The ease with which the hPrP structure can, accommodate a variety of locations for a second disulfide bond within the, presumed protein X-binding epitope suggests a functional role for the, extensive perturbation by a natural second disulfide bond of the, corresponding region in the human doppel protein.
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
1H0L is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
NMR structure of a variant human prion protein with two disulfide bridges., Zahn R, Guntert P, von Schroetter C, Wuthrich K, J Mol Biol. 2003 Feb 7;326(1):225-34. PMID:12547204
Page seeded by OCA on Fri Feb 15 15:55:05 2008
