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PDBsum entry 1tfp
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protein ligands Protein-protein interface(s) links
Transport (thyroxine) PDB id
1tfp

 

 

 

 

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Contents
Protein chains
114 a.a. *
Ligands
SO4
Waters ×1
* Residue conservation analysis
PDB id:
1tfp
Name: Transport (thyroxine)
Title: Transthyretin (formerly known as prealbumin)
Structure: Transthyretin. Chain: a, b. Synonym: prealbumin
Source: Gallus gallus. Chicken. Organism_taxid: 9031. Tissue: serum
Resolution:
2.90Å     R-factor:   0.199    
Authors: M.Sunde,S.J.Richardson,L.Chang,T.M.Pettersson,G.Schreiber,C.C.F.Blake
Key ref: M.Sunde et al. (1996). The crystal structure of transthyretin from chicken. Eur J Biochem, 236, 491-499. PubMed id: 8612621
Date:
05-Jan-96     Release date:   10-Jun-96    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P27731  (TTHY_CHICK) -  Transthyretin from Gallus gallus
Seq:
Struc: 		150 a.a.
114 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
Eur J Biochem 236:491-499 (1996)
PubMed id: 8612621  
 
 
The crystal structure of transthyretin from chicken.
M.Sunde, S.J.Richardson, L.Chang, T.M.Pettersson, G.Schreiber, C.C.Blake.
 
  ABSTRACT  
 
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.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20133122 S.Connelly, S.Choi, S.M.Johnson, J.W.Kelly, and I.A.Wilson (2010).
Structure-based design of kinetic stabilizers that ameliorate the transthyretin amyloidoses.
  Curr Opin Struct Biol, 20, 54-62.  
19250316 E.Lundberg, A.Olofsson, G.T.Westermark, and A.E.Sauer-Eriksson (2009).
Stability and fibril formation properties of human and fish transthyretin, and of the Escherichia coli transthyretin-related protein.
  FEBS J, 276, 1999-2011.  
19725883 P.Prapunpoj, and L.Leelawatwattana (2009).
Evolutionary changes to transthyretin: structure-function relationships.
  FEBS J, 276, 5330-5341.  
19725880 S.C.Hennebry (2009).
Evolutionary changes to transthyretin: structure and function of a transthyretin-like ancestral protein.
  FEBS J, 276, 5367-5379.  
19021760 G.Zanotti, C.Folli, L.Cendron, B.Alfieri, S.K.Nishida, F.Gliubich, N.Pasquato, A.Negro, and R.Berni (2008).
Structural and mutational analyses of protein-protein interactions between transthyretin and retinol-binding protein.
  FEBS J, 275, 5841-5854.
PDB codes: 3bsz 3bt0 3cxf
18550270 S.J.Richardson (2008).
Marsupial models for understanding evolution of thyroid hormone distributor proteins.
  Mol Cell Endocrinol, 293, 32-42.  
15082720 T.Eneqvist, E.Lundberg, A.Karlsson, S.Huang, C.R.Santos, D.M.Power, and A.E.Sauer-Eriksson (2004).
High resolution crystal structures of piscine transthyretin reveal different binding modes for triiodothyronine and thyroxine.
  J Biol Chem, 279, 26411-26416.
PDB codes: 1sn0 1sn2 1sn5
12542701 T.Eneqvist, E.Lundberg, L.Nilsson, R.Abagyan, and A.E.Sauer-Eriksson (2003).
The transthyretin-related protein family.
  Eur J Biochem, 270, 518-532.  
12553423 H.L.Monaco (2002).
Three-dimensional structure of the transthyretin-retinol-binding protein complex.
  Clin Chem Lab Med, 40, 1229-1236.  
12553419 S.J.Richardson (2002).
The evolution of transthyretin synthesis in vertebrate liver, in primitive eukaryotes and in bacteria.
  Clin Chem Lab Med, 40, 1191-1199.  
11468389 A.Wojtczak, V.Cody, J.R.Luft, and W.Pangborn (2001).
Structure of rat transthyretin (rTTR) complex with thyroxine at 2.5 A resolution: first non-biased insight into thyroxine binding reveals different hormone orientation in two binding sites.
  Acta Crystallogr D Biol Crystallogr, 57, 1061-1070.
PDB code: 1ie4
  11676293 T.Eneqvist, and A.E.Sauer-Eriksson (2001).
Structural distribution of mutations associated with familial amyloidotic polyneuropathy in human transthyretin.
  Amyloid, 8, 149-168.  
11058748 H.L.Monaco (2000).
The transthyretin-retinol-binding protein complex.
  Biochim Biophys Acta, 1482, 65-72.  
10089423 G.Malpeli, G.Zanotti, F.Gliubich, A.Rizzotto, S.K.Nishida, C.Folli, and R.Berni (1999).
Crystallization and preliminary X-ray data for the human transthyretin-retinol-binding protein (RBP) complex bound to an anti-RBP Fab.
  Acta Crystallogr D Biol Crystallogr, 55, 276-278.  
9914537 L.Chang, S.L.Munro, S.J.Richardson, and G.Schreiber (1999).
Evolution of thyroid hormone binding by transthyretins in birds and mammals.
  Eur J Biochem, 259, 534-542.  
9208931 A.R.Aldred, P.Prapunpoj, and G.Schreiber (1997).
Evolution of shorter and more hydrophilic transthyretin N-termini by stepwise conversion of exon 2 into intron 1 sequences (shifting the 3' splice site of intron 1)
  Eur J Biochem, 246, 401-409.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.

 

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