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PDBsum entry 1tfp
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Transport (thyroxine)
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PDB id
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1tfp
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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The crystal structure of transthyretin from chicken.
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Authors
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M.Sunde,
S.J.Richardson,
L.Chang,
T.M.Pettersson,
G.Schreiber,
C.C.Blake.
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Ref.
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Eur J Biochem, 1996,
236,
491-499.
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PubMed id
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Note In the PDB file this reference is
annotated as "TO BE PUBLISHED".
The citation details given above were identified by an automated
search of PubMed on title and author
names, giving a
perfect match.
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Abstract
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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.
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Secondary reference #1
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Title
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Structure of prealbumin: secondary, Tertiary and quaternary interactions determined by fourier refinement at 1.8 a.
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Authors
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C.C.Blake,
M.J.Geisow,
S.J.Oatley,
B.Rérat,
C.Rérat.
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Ref.
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J Mol Biol, 1978,
121,
339-356.
[DOI no: ]
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PubMed id
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Figure 7.
FIG. 7. Stereo drawg of he nternal water structure. Thick and thin lines isinuih the 2
rnonorners n the dimer. a) Shows the hydrogen ond network involving he water molecules,
and b) their local nvironment in he imer.
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Figure 11.
FIQ. 11. Stereo drawing of the association of he DAGHH''A'U' hot% from ach ime1
looking down the axis with own and acmss. It, s n quivalent view t,o ig. (a) and the
right-hand diagram of Fig. 9. The imer-dimw inbfaces arc ocated at, he edges of his truct,nrr.
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The above figures are
reproduced from the cited reference
with permission from Elsevier
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