Database accession: MF4110002
Name: Transthyretin (Sparus aurata)
PDB ID: 1oo2
Experimental method: X-ray (1.56 Å)
Assembly: Homotetramer
Source organism: Sparus aurata
Primary publication of the structure:
Folli C, Pasquato N, Ramazzina I, Battistutta R, Zanotti G, Berni R
Distinctive binding and structural properties of piscine transthyretin.
(2003) FEBS Lett. 555: 279-84
PMID: 14644428
Abstract:
The thyroid hormone binding protein transthyretin (TTR) forms a macromolecular complex with the retinol-specific carrier retinol binding protein (RBP) in the blood of higher vertebrates. Piscine TTR is shown here to exhibit high binding affinity for L-thyroxine and negligible affinity for RBP. The 1.56 A resolution X-ray structure of sea bream TTR, compared with that of human TTR, reveals a high degree of conservation of the thyroid hormone binding sites. In contrast, some amino acid differences in discrete regions of sea bream TTR appear to be responsible for the lack of protein-protein recognition, providing evidence for the crucial role played by a limited number of residues in the interaction between RBP and TTR. Overall, this study makes it possible to draw conclusions on evolutionary relationships for RBPs and TTRs of phylogenetically distant vertebrates.
Annotations from the GeneOntology database. Only terms that fit at least two of the interacting proteins are shown. Molecular function:
hormone activity hormone activity
thyroid hormone binding thyroid hormone binding
Biological process:
purine nucleobase metabolic process purine nucleobase metabolic process
Cellular component:
extracellular space extracellular space
Structural annotations of the participating protein chains.Entry contents: 4 distinct polypeptide molecules
Chains: A, B, C, D
Notes: All chains according to the most probable oligomerization state stored in PDBe were considered.
Number of unique protein segments: 1
Name: Transthyretin
Source organism: Sparus aurata
Length: 151 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMLQPLHCLLLASAVLLCNTAPTPTDKHGGSDTRCPLMVKILDAVKGTPAGSVALKVSQKTADGGWTQIATGVTDATGEIHNLITEQQFPAGVYRVEFDTKAYWTNQGSTPFHEVAEVVFDAHPEGHRHYTLALLLSPFSYTTTAVVSSVRE
UniProtKB AC: Q9PTT3 (positions: 33-148)
Coverage: 76%
Name: Transthyretin
Source organism: Sparus aurata
Length: 151 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMLQPLHCLLLASAVLLCNTAPTPTDKHGGSDTRCPLMVKILDAVKGTPAGSVALKVSQKTADGGWTQIATGVTDATGEIHNLITEQQFPAGVYRVEFDTKAYWTNQGSTPFHEVAEVVFDAHPEGHRHYTLALLLSPFSYTTTAVVSSVRE
UniProtKB AC: Q9PTT3 (positions: 33-148)
Coverage: 76%
Name: Transthyretin
Source organism: Sparus aurata
Length: 151 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMLQPLHCLLLASAVLLCNTAPTPTDKHGGSDTRCPLMVKILDAVKGTPAGSVALKVSQKTADGGWTQIATGVTDATGEIHNLITEQQFPAGVYRVEFDTKAYWTNQGSTPFHEVAEVVFDAHPEGHRHYTLALLLSPFSYTTTAVVSSVRE
UniProtKB AC: Q9PTT3 (positions: 33-148)
Coverage: 76%
Name: Transthyretin
Source organism: Sparus aurata
Length: 151 residues
Sequence:Sequence according to the corresponding UniProt protein segmentMLQPLHCLLLASAVLLCNTAPTPTDKHGGSDTRCPLMVKILDAVKGTPAGSVALKVSQKTADGGWTQIATGVTDATGEIHNLITEQQFPAGVYRVEFDTKAYWTNQGSTPFHEVAEVVFDAHPEGHRHYTLALLLSPFSYTTTAVVSSVRE
UniProtKB AC: Q9PTT3 (positions: 33-148)
Coverage: 76%
Evidence demonstrating that the participating proteins are unstructured prior to the interaction and their folding is coupled to binding. Representative domain in related structures: HIUase/Transthyretin family
Evidence level: Direct evidence
Evidence coverage: The full structure participates in mutual synergistic folding.
Complex Evidence:
Transthyretin was shown in calorimetrics experiments to follow two-state folding/binding kinetics with the emergence of structure being linked to oligomerization (PMID:11152276).
Chain A:
N/A
Chain B:
N/A
Chain C:
N/A
Chain D:
N/A
Surface and contacts features:
Structures from the PDB that contain the same number of proteins, and the proteins from the two structures show a sufficient degree of pairwise similarity, i.e. they belong to the same UniRef90 cluster (the full proteins exhibit at least 90% sequence identity) and convey roughly the same region to their respective interactions (the two regions from the two proteins share a minimum of 70% overlap). Download the CIF file (.cif)
Download this entry's XML file (.xml)
Download this entry's JSON file (.json)
