PDBsum entry 3bt0

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protein Protein-protein interface(s) links
Transport protein PDB id
Protein chain
116 a.a. *
Waters ×140
* Residue conservation analysis
PDB id:
Name: Transport protein
Title: Crystal structure of transthyretin variant v20s
Structure: Transthyretin. Chain: a, b. Synonym: prealbumin, tbpa, ttr, attr. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.
1.59Å     R-factor:   0.210     R-free:   0.229
Authors: G.Zanotti,C.Folli,L.Cendron,F.Gliubich,A.Negro,R.Berni
Key ref: G.Zanotti et al. (2008). Structural and mutational analyses of protein-protein interactions between transthyretin and retinol-binding protein. FEBS J, 275, 5841-5854. PubMed id: 19021760
27-Dec-07     Release date:   11-Nov-08    
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Protein chains
Pfam   ArchSchema ?
P02766  (TTHY_HUMAN) -  Transthyretin
147 a.a.
116 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   5 terms 
  Biological process     transport   5 terms 
  Biochemical function     protein binding     5 terms  


FEBS J 275:5841-5854 (2008)
PubMed id: 19021760  
Structural and mutational analyses of protein-protein interactions between transthyretin and retinol-binding protein.
G.Zanotti, C.Folli, L.Cendron, B.Alfieri, S.K.Nishida, F.Gliubich, N.Pasquato, A.Negro, R.Berni.
Transthyretin is a tetrameric binding protein involved in the transport of thyroid hormones and in the cotransport of retinol by forming a complex in plasma with retinol-binding protein. In the present study, we report the crystal structure of a macromolecular complex, in which human transthyretin, human holo-retinol-binding protein and a murine anti-retinol-binding protein Fab are assembled according to a 1 : 2 : 2 stoichiometry. The main interactions, both polar and apolar, between retinol-binding protein and transthyretin involve the retinol hydroxyl group and a limited number of solvent exposed residues. The relevance of transthyretin residues in complex formation with retinol-binding protein has been examined by mutational analysis, and the structural consequences of some transthyretin point mutations affecting protein-protein recognition have been investigated. Despite a few exceptions, in general, the substitution of a hydrophilic for a hydrophobic side chain in contact regions results in a decrease or even a loss of binding affinity, thus revealing the importance of interfacial hydrophobic interactions and a high degree of complementarity between retinol-binding protein and transthyretin. The effect is particularly evident when the mutation affects an interacting residue present in two distinct subunits of transthyretin participating simultaneously in two interactions with a retinol-binding protein molecule. This is the case of the amyloidogenic I84S replacement, which abolishes the interaction with retinol-binding protein and is associated with an altered retinol-binding protein plasma transport in carriers of this mutation. Remarkably, some of the residues in mutated human transthyretin that weaken or abolish the interaction with retinol-binding protein are present in piscine transthyretin, consistent with the lack of interaction between retinol-binding protein and transthyretin in fish.

Literature references that cite this PDB file's key reference

  PubMed id Reference
22120744 V.A.Rao, S.M.Shepherd, G.English, S.J.Coulthurst, and W.N.Hunter (2011).
The structure of Serratia marcescens Lip, a membrane-bound component of the type VI secretion system.
  Acta Crystallogr D Biol Crystallogr, 67, 1065-1072.
PDB code: 4a1r
19602727 L.Cendron, A.Trovato, F.Seno, C.Folli, B.Alfieri, G.Zanotti, and R.Berni (2009).
Amyloidogenic potential of transthyretin variants: insights from structural and computational analyses.
  J Biol Chem, 284, 25832-25841.
PDB codes: 3djr 3djs 3djt 3djz 3dk0 3dk2
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