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.


1tqc

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1tqc.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1tqc.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1tqc| PDB=1tqc | SCENE= }}
{{STRUCTURE_1tqc| PDB=1tqc | SCENE= }}
-
'''Ovine recombinant PrP(114-234), ARR variant in complex with the VRQ14 Fab fragment (IgG2a)'''
+
===Ovine recombinant PrP(114-234), ARR variant in complex with the VRQ14 Fab fragment (IgG2a)===
-
==Overview==
+
<!--
-
Prion diseases are associated with the conversion of the alpha-helix rich prion protein (PrPC) into a beta-structure-rich insoluble conformer (PrPSc) that is thought to be infectious. The mechanism for the PrPC--&gt;PrPSc conversion and its relationship with the pathological effects of prion diseases are poorly understood, partly because of our limited knowledge of the structure of PrPSc. In particular, the way in which mutations in the PRNP gene yield variants that confer different susceptibilities to disease needs to be clarified. We report here the 2.5-A-resolution crystal structures of three scrapie-susceptibility ovine PrP variants complexed with an antibody that binds to PrPC and to PrPSc; they identify two important features of the PrPC--&gt;PrPSc conversion. First, the epitope of the antibody mainly consists of the last two turns of ovine PrP second alpha-helix. We show that this is a structural invariant in the PrPC--&gt;PrPSc conversion; taken together with biochemical data, this leads to a model of the conformational change in which the two PrPC C-terminal alpha-helices are conserved in PrPSc, whereas secondary structure changes are located in the N-terminal alpha-helix. Second, comparison of the structures of scrapie-sensitivity variants defines local changes in distant parts of the protein that account for the observed differences of PrPC stability, resistant variants being destabilized compared with sensitive ones. Additive contributions of these sensitivity-modulating mutations to resistance suggest a possible causal relationship between scrapie resistance and lowered stability of the PrP protein.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15240887}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15240887 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15240887}}
==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Antibody]]
[[Category: Antibody]]
[[Category: Prion]]
[[Category: Prion]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:14:59 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 05:50:00 2008''

Revision as of 02:50, 28 July 2008

Image:1tqc.png

Template:STRUCTURE 1tqc

Ovine recombinant PrP(114-234), ARR variant in complex with the VRQ14 Fab fragment (IgG2a)

Template:ABSTRACT PUBMED 15240887

About this Structure

1TQC is a Single protein structure of sequence from Mus musculus and Ovis aries. Full crystallographic information is available from OCA.

Reference

Insight into the PrPC-->PrPSc conversion from the structures of antibody-bound ovine prion scrapie-susceptibility variants., Eghiaian F, Grosclaude J, Lesceu S, Debey P, Doublet B, Treguer E, Rezaei H, Knossow M, Proc Natl Acad Sci U S A. 2004 Jul 13;101(28):10254-9. Epub 2004 Jul 6. PMID:15240887

Page seeded by OCA on Mon Jul 28 05:50:00 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1tqc"
Personal tools