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| [[Image:5ttr.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_5ttr| PDB=5ttr | SCENE= }} | | {{STRUCTURE_5ttr| PDB=5ttr | SCENE= }} |
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| '''LEU 55 PRO TRANSTHYRETIN CRYSTAL STRUCTURE'''
| | ===LEU 55 PRO TRANSTHYRETIN CRYSTAL STRUCTURE=== |
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| ==Overview==
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| 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. | | The line below this paragraph, {{ABSTRACT_PUBMED_9733771}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 9733771 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_9733771}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Transport]] | | [[Category: Transport]] |
| [[Category: Transthyretin]] | | [[Category: Transthyretin]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:38:19 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 14:12:32 2008'' |
