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.


1fhn

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1fhn.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1fhn.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1fhn| PDB=1fhn | SCENE= }}
{{STRUCTURE_1fhn| PDB=1fhn | SCENE= }}
-
'''TRANSTHYRETIN STABILITY AS A KEY FACTOR IN AMYLOIDOGENESIS'''
+
===TRANSTHYRETIN STABILITY AS A KEY FACTOR IN AMYLOIDOGENESIS===
-
==Overview==
+
<!--
-
Transthyretin (TTR) amyloidosis is a conformational disturbance, which, like other amyloidoses, represents a life threat. Here, we report a TTR variant, TTR Thr119Met, that has been shown to have a protective role in the development of clinical symptoms in carriers of TTR Val30Met, one of the most frequent variants among TTR amyloidosis patients. In order to understand this effect, we have determined the structures of the TTR Val30Met/Thr119Met double mutant isolated from the serum of one patient and of both the native and thyroxine complex of TTR Thr119Met. Major conclusions are: (i) new H-bonds within each monomer and monomer-monomer inter-subunit contacts, e.g. Ser117-Ser117 and Met119-Tyr114, increase protein stability, possibly leading to the protective effect of the TTR Val30Met/Thr119Met variant when compared to the single variant TTR Val30Met. (ii) The mutated residue (Met119) extends across the thyroxine binding channel inducing conformational changes that lead to closer contacts between different dimers within the tetramer. The data, at atomic resolution, were essential to detect, for the first time, the subtle changes in the inter-subunit contacts of TTR, and explain the non-amyloidogenic potential of the TTR Thr119Met variant, improving considerably current research on the TTR amyloid fibril formation pathway.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11243784}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11243784 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11243784}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Transthyretin]]
[[Category: Transthyretin]]
[[Category: X-ray crystallography]]
[[Category: X-ray crystallography]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:20:07 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 03:15:38 2008''

Revision as of 00:15, 1 July 2008

Image:1fhn.png

Template:STRUCTURE 1fhn

TRANSTHYRETIN STABILITY AS A KEY FACTOR IN AMYLOIDOGENESIS

Template:ABSTRACT PUBMED 11243784

About this Structure

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

Reference

Transthyretin stability as a key factor in amyloidogenesis: X-ray analysis at atomic resolution., Sebastiao MP, Lamzin V, Saraiva MJ, Damas AM, J Mol Biol. 2001 Mar 2;306(4):733-44. PMID:11243784

Page seeded by OCA on Tue Jul 1 03:15:38 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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