This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1h0l
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1h0l.jpg|left|200px]] | [[Image:1h0l.jpg|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1h0l", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | | | + | or leave the SCENE parameter empty for the default display. |
| - | | | + | --> |
| - | + | {{STRUCTURE_1h0l| PDB=1h0l | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''HUMAN PRION PROTEIN 121-230 M166C/E221C''' | '''HUMAN PRION PROTEIN 121-230 M166C/E221C''' | ||
| Line 28: | Line 25: | ||
[[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: Major prion protein]] |
| - | [[Category: | + | [[Category: Polymorphism]] |
| - | [[Category: | + | [[Category: Prion]] |
| - | [[Category: | + | [[Category: Prion protein]] |
| - | [[Category: | + | [[Category: Repeat]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:15:39 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 15:15, 2 May 2008
HUMAN PRION PROTEIN 121-230 M166C/E221C
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.
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 May 2 18:15:39 2008
