1x7t

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{{STRUCTURE_1x7t| PDB=1x7t | SCENE= }}
{{STRUCTURE_1x7t| PDB=1x7t | SCENE= }}
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'''Structure of TTR R104H: a non-amyloidogenic variant with protective clinical effects'''
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===Structure of TTR R104H: a non-amyloidogenic variant with protective clinical effects===
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==Overview==
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Transthyretin (TTR) is a homotetrameric plasma protein that, as a result of a set of not yet fully characterized conformational changes, forms fibrillar aggregates that are the major protein component of amyloid deposits. More than 80 mutations associated with TTR amyloid deposition have been described in the literature. X-ray crystallography was used to elucidate the three-dimensional structure of two important TTR variants: TTR Y78F, an amyloidogenic protein, and TTR R104H, which is associated with a protective effect over the amyloidogenic V30M mutation. The structures of those two TTR variants have been determined in space group P2(1)2(1)2 to 1.55 and 1.60 angstroms resolution, respectively, using molecular-replacement techniques. Detailed analysis of the protein model for TTR Y78F indicates a destabilization of the contacts between the alpha-helix and AB loop and the body of the molecule, intimately related to the amyloidogenic nature; contrastingly, in the TTR R104H variant new contacts involving the N-terminal region and His104 are clearly antagonists of amyloid formation.
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(as it appears on PubMed at http://www.pubmed.gov), where 15735344 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15735344}}
==About this Structure==
==About this Structure==
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[[Category: Transthyretin]]
[[Category: Transthyretin]]
[[Category: X-ray crystallography]]
[[Category: X-ray crystallography]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 03:40:00 2008''

Revision as of 00:40, 28 July 2008

Image:1x7t.png

Template:STRUCTURE 1x7t

Structure of TTR R104H: a non-amyloidogenic variant with protective clinical effects

Template:ABSTRACT PUBMED 15735344

About this Structure

1X7T is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

X-ray crystallographic studies of two transthyretin variants: further insights into amyloidogenesis., Neto-Silva RM, Macedo-Ribeiro S, Pereira PJ, Coll M, Saraiva MJ, Damas AM, Acta Crystallogr D Biol Crystallogr. 2005 Mar;61(Pt 3):333-9. Epub 2005, Feb 24. PMID:15735344

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