1tfp
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TRANSTHYRETIN (FORMERLY KNOWN AS PREALBUMIN)
OverviewOverview
The crystal structure of chicken transthyretin has been solved at 290-pm, resolution by molecular-replacement techniques. Transthyretin is the, protein component of the amyloid fibrils found in patients suffering from, either familial amyloidotic polyneuropathy or senile systemic amyloidosis., Familial amyloidotic polyneuropathy is an autosomal dominant hereditary, type of amyloidosis which involves transthyretin with either one or two, amino acid substitutions. The three-dimensional structure of chicken, transthyretin was determined in order to compare a non-amyloidogenic, species-variant transthyretin with wild-type and mutant transthyretin, molecules. Of the 31 chicken-to-human residue differences, 9 occur at, positions which in human transthyretin give rise to amyloidogenic variants, although none corresponds to the appropriate side-chain substitutions. The, model of chicken transthyretin has been refined to an R-factor of 19.9%., The overall fold of the protein is that of an all-beta protein. Compared, with wild-type human transthyretin the avian transthyretin shows quite, large differences in the region known to be involved in binding to, retinol-binding protein, it has a much shorter helical component than the, human protein and some of the monomer-monomer interactions are different.
About this StructureAbout this Structure
1TFP is a Single protein structure of sequence from Gallus gallus with SO4 as ligand. Full crystallographic information is available from OCA.
ReferenceReference
The crystal structure of transthyretin from chicken., Sunde M, Richardson SJ, Chang L, Pettersson TM, Schreiber G, Blake CC, Eur J Biochem. 1996 Mar 1;236(2):491-9. PMID:8612621
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