1h0l
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1h0l.jpg|left|200px]] | + | [[Image:1h0l.jpg|left|200px]] |
| - | + | ||
| - | '''HUMAN PRION PROTEIN 121-230 M166C/E221C''' | + | {{Structure |
| + | |PDB= 1h0l |SIZE=350|CAPTION= <scene name='initialview01'>1h0l</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''HUMAN PRION PROTEIN 121-230 M166C/E221C''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 10: | Line 19: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1H0L is a [ | + | 1H0L is a [[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== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12547204 12547204] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 29: | Line 38: | ||
[[Category: repeat]] | [[Category: repeat]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:30:32 2008'' |
Revision as of 09:30, 20 March 2008
| |||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Thu Mar 20 11:30:32 2008
