5ttr: Difference between revisions
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'''LEU 55 PRO TRANSTHYRETIN CRYSTAL STRUCTURE''' | '''LEU 55 PRO TRANSTHYRETIN CRYSTAL STRUCTURE''' | ||
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[[Category: Saraiva, M J.]] | [[Category: Saraiva, M J.]] | ||
[[Category: Sebastiao, M P.]] | [[Category: Sebastiao, M P.]] | ||
[[Category: | [[Category: Amyloid]] | ||
[[Category: | [[Category: Crystal structure]] | ||
[[Category: | [[Category: Fap]] | ||
[[Category: | [[Category: Thyroxine]] | ||
[[Category: | [[Category: Transport]] | ||
[[Category: | [[Category: Transthyretin]] | ||
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Revision as of 19:38, 4 May 2008
LEU 55 PRO TRANSTHYRETIN CRYSTAL STRUCTURE
Overview
The x-ray crystal structure of the amyloidogenic Leu55 --> Pro transthyretin (TTR) variant, implicated as the causative agent in early-onset familial amyloidotic polyneuropathy (Jacobson, D. R., McFarlin, D. E., Kane, I., and Buxbaum, J. N. (1992) Hum. Genet. 89, 353-356), has been solved by molecular replacement, refined at 2.7 A to a Rcryst value of 0.190 (Fobs > 2.0sigma), and compared with wild-type transthyretin to understand the molecular mechanism(s) involved in amyloidogenesis. Leu55 --> Pro TTR crystallizes in space group C2, with eight monomers in the asymmetric unit, and the observed packing contacts are considerably different from those described for the wild-type protein. Refinement of the crystal structure shows that the proline for leucine substitution disrupts the hydrogen bonds between strands D and A, resulting in different interface contacts. Based on the assumption that the observed packing contacts may be significant for amyloidogenesis, a model for the TTR amyloid is proposed. It consists of a tubular structure with inner and outer diameters approximately of 30 and 100 A and four monomers per cross-section.
About this Structure
5TTR is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The crystal structure of amyloidogenic Leu55 --> Pro transthyretin variant reveals a possible pathway for transthyretin polymerization into amyloid fibrils., Sebastiao MP, Saraiva MJ, Damas AM, J Biol Chem. 1998 Sep 18;273(38):24715-22. PMID:9733771 Page seeded by OCA on Sun May 4 22:38:19 2008
