1sn0
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==Crystal Structure Of Sea Bream Transthyretin in complex with thyroxine At 1.9A Resolution== | ==Crystal Structure Of Sea Bream Transthyretin in complex with thyroxine At 1.9A Resolution== | ||
| - | <StructureSection load='1sn0' size='340' side='right' caption='[[1sn0]], [[Resolution|resolution]] 1.90Å' scene=''> | + | <StructureSection load='1sn0' size='340' side='right'caption='[[1sn0]], [[Resolution|resolution]] 1.90Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | [[1sn0]] is a 4 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1sn0]] 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=1SN0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SN0 FirstGlance]. <br> |
| - | <b>[[Ligand|Ligands:]]</b> <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=T44:3,5,3,5-TETRAIODO-L-THYRONINE'>T44</scene>< | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=T44:3,5,3,5-TETRAIODO-L-THYRONINE'>T44</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=1sn0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sn0 OCA], [https://pdbe.org/1sn0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sn0 RCSB], [https://www.ebi.ac.uk/pdbsum/1sn0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sn0 ProSAT]</span></td></tr> |
| - | <b>Resources:</b> <span class='plainlinks'>[ | + | </table> |
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q9PTT3_SPAAU Q9PTT3_SPAAU] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
| - | [[Image:Consurf_key_small.gif|right]] | + | [[Image:Consurf_key_small.gif|200px|right]] |
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/sn/1sn0_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/sn/1sn0_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/ | + | </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=1sn0 ConSurf]. |
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Transthyretin (TTR) is an extracellular transport protein involved in the distribution of thyroid hormones and vitamin A. So far, TTR has only been found in vertebrates, of which piscine TTR displays the lowest sequence identity with human TTR (47%). Human and piscine TTR bind both thyroid hormones 3,5,3'-triiodo-l-thyronine (T(3)) and 3,5,3',5'-tetraiodo-l-thyronine (thyroxine, T(4)). Human TTR has higher affinity for T(4) than T(3), whereas the reverse holds for piscine TTR. X-ray structures of Sparus aurata (sea bream) TTR have been determined as the apo-protein at 1.75 A resolution and bound to ligands T(3) and T(4), both at 1.9 A resolution. The apo structure is similar to human TTR with structural changes only at beta-strand D. This strand forms an extended loop conformation similar to the one in chicken TTR. The piscine TTR.T(4) complex shows the T(4)-binding site to be similar but not identical to human TTR, whereas the TTR.T(3) complex shows the I3' halogen situated at the site normally occupied by the hydroxyl group of T(4). The significantly wider entrance of the hormone-binding channel in sea bream TTR, in combination with its narrower cavity, provides a structural explanation for the different binding affinities of human and piscine TTR to T(3) and T(4). | Transthyretin (TTR) is an extracellular transport protein involved in the distribution of thyroid hormones and vitamin A. So far, TTR has only been found in vertebrates, of which piscine TTR displays the lowest sequence identity with human TTR (47%). Human and piscine TTR bind both thyroid hormones 3,5,3'-triiodo-l-thyronine (T(3)) and 3,5,3',5'-tetraiodo-l-thyronine (thyroxine, T(4)). Human TTR has higher affinity for T(4) than T(3), whereas the reverse holds for piscine TTR. X-ray structures of Sparus aurata (sea bream) TTR have been determined as the apo-protein at 1.75 A resolution and bound to ligands T(3) and T(4), both at 1.9 A resolution. The apo structure is similar to human TTR with structural changes only at beta-strand D. This strand forms an extended loop conformation similar to the one in chicken TTR. The piscine TTR.T(4) complex shows the T(4)-binding site to be similar but not identical to human TTR, whereas the TTR.T(3) complex shows the I3' halogen situated at the site normally occupied by the hydroxyl group of T(4). The significantly wider entrance of the hormone-binding channel in sea bream TTR, in combination with its narrower cavity, provides a structural explanation for the different binding affinities of human and piscine TTR to T(3) and T(4). | ||
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High resolution crystal structures of piscine transthyretin reveal different binding modes for triiodothyronine and thyroxine.,Eneqvist T, Lundberg E, Karlsson A, Huang S, Santos CR, Power DM, Sauer-Eriksson AE J Biol Chem. 2004 Jun 18;279(25):26411-6. Epub 2004 Apr 13. PMID:15082720<ref>PMID:15082720</ref> | High resolution crystal structures of piscine transthyretin reveal different binding modes for triiodothyronine and thyroxine.,Eneqvist T, Lundberg E, Karlsson A, Huang S, Santos CR, Power DM, Sauer-Eriksson AE J Biol Chem. 2004 Jun 18;279(25):26411-6. Epub 2004 Apr 13. PMID:15082720<ref>PMID:15082720</ref> | ||
| - | From | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| + | </div> | ||
| + | <div class="pdbe-citations 1sn0" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Transthyretin 3D structures|Transthyretin 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Eneqvist | + | [[Category: Sparus aurata]] |
| - | [[Category: Huang | + | [[Category: Eneqvist T]] |
| - | [[Category: Karlsson | + | [[Category: Huang S]] |
| - | [[Category: Lundberg | + | [[Category: Karlsson A]] |
| - | [[Category: Power | + | [[Category: Lundberg E]] |
| - | [[Category: Santos | + | [[Category: Power DM]] |
| - | [[Category: Sauer-Eriksson | + | [[Category: Santos CR]] |
| - | + | [[Category: Sauer-Eriksson AE]] | |
Current revision
Crystal Structure Of Sea Bream Transthyretin in complex with thyroxine At 1.9A Resolution
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