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| | <StructureSection load='1oo2' size='340' side='right'caption='[[1oo2]], [[Resolution|resolution]] 1.56Å' scene=''> | | <StructureSection load='1oo2' size='340' side='right'caption='[[1oo2]], [[Resolution|resolution]] 1.56Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1oo2]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Aurata_aurata Aurata aurata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OO2 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1OO2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1oo2]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Sparus_aurata Sparus aurata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OO2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OO2 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.56Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1fhn|1fhn]], [[1f41|1f41]], [[1rlb|1rlb]], [[1qab|1qab]], [[1ie4|1ie4]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TTR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8175 Aurata aurata])</td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1oo2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oo2 OCA], [https://pdbe.org/1oo2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oo2 RCSB], [https://www.ebi.ac.uk/pdbsum/1oo2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oo2 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1oo2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oo2 OCA], [http://pdbe.org/1oo2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1oo2 RCSB], [http://www.ebi.ac.uk/pdbsum/1oo2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1oo2 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9PTT3_SPAAU Q9PTT3_SPAAU] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Aurata aurata]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Battistutta, R]] | + | [[Category: Sparus aurata]] |
| - | [[Category: Berni, R]] | + | [[Category: Battistutta R]] |
| - | [[Category: Folli, C]] | + | [[Category: Berni R]] |
| - | [[Category: Pasquato, N]] | + | [[Category: Folli C]] |
| - | [[Category: Ramazzina, I]] | + | [[Category: Pasquato N]] |
| - | [[Category: Zanotti, G]] | + | [[Category: Ramazzina I]] |
| - | [[Category: Retinol-binding protein]]
| + | [[Category: Zanotti G]] |
| - | [[Category: Tetramer]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| - | [[Category: Transthyretin]]
| + | |
| Structural highlights
Function
Q9PTT3_SPAAU
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Distinctive binding and structural properties of piscine transthyretin.,Folli C, Pasquato N, Ramazzina I, Battistutta R, Zanotti G, Berni R FEBS Lett. 2003 Dec 4;555(2):279-84. PMID:14644428[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Folli C, Pasquato N, Ramazzina I, Battistutta R, Zanotti G, Berni R. Distinctive binding and structural properties of piscine transthyretin. FEBS Lett. 2003 Dec 4;555(2):279-84. PMID:14644428
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