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[[Image:1oo2.gif|left|200px]]
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{{STRUCTURE_1oo2|  PDB=1oo2  |  SCENE=  }}
'''Crystal structure of transthyretin from Sparus aurata'''


==Crystal structure of transthyretin from Sparus aurata==
<StructureSection load='1oo2' size='340' side='right'caption='[[1oo2]], [[Resolution|resolution]] 1.56&Aring;' scene=''>
== Structural highlights ==
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.56&#8491;</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='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>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9PTT3_SPAAU Q9PTT3_SPAAU]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oo/1oo2_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1oo2 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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.


==Overview==
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<ref>PMID:14644428</ref>
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.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1OO2 is a [[Single protein]] structure of sequence from [http://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].
</div>
<div class="pdbe-citations 1oo2" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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:[http://www.ncbi.nlm.nih.gov/pubmed/14644428 14644428]
*[[Transthyretin 3D structures|Transthyretin 3D structures]]
[[Category: Single protein]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Sparus aurata]]
[[Category: Sparus aurata]]
[[Category: Battistutta, R.]]
[[Category: Battistutta R]]
[[Category: Berni, R.]]
[[Category: Berni R]]
[[Category: Folli, C.]]
[[Category: Folli C]]
[[Category: Pasquato, N.]]
[[Category: Pasquato N]]
[[Category: Ramazzina, I.]]
[[Category: Ramazzina I]]
[[Category: Zanotti, G.]]
[[Category: Zanotti G]]
[[Category: Retinol-binding protein]]
[[Category: Tetramer]]
[[Category: Transthyretin]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 04:05:16 2008''
Retrieved from "https://proteopedia.org/1oo2"