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1tfp

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[[Image:1tfp.gif|left|200px]]
 
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{{Structure
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==TRANSTHYRETIN (FORMERLY KNOWN AS PREALBUMIN)==
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|PDB= 1tfp |SIZE=350|CAPTION= <scene name='initialview01'>1tfp</scene>, resolution 2.9&Aring;
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<StructureSection load='1tfp' size='340' side='right'caption='[[1tfp]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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<table><tr><td colspan='2'>[[1tfp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TFP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TFP FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1tfp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tfp OCA], [https://pdbe.org/1tfp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tfp RCSB], [https://www.ebi.ac.uk/pdbsum/1tfp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tfp ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tfp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tfp OCA], [http://www.ebi.ac.uk/pdbsum/1tfp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tfp RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/TTHY_CHICK TTHY_CHICK] Thyroid hormone-binding protein. Probably transports thyroxine from the bloodstream to the brain.<ref>PMID:1833190</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tf/1tfp_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1tfp ConSurf].
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<div style="clear:both"></div>
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'''TRANSTHYRETIN (FORMERLY KNOWN AS PREALBUMIN)'''
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==See Also==
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*[[Transthyretin 3D structures|Transthyretin 3D structures]]
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== References ==
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==Overview==
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<references/>
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The crystal structure of chicken transthyretin has been solved at 290-pm resolution by molecular-replacement techniques. Transthyretin is the protein component of the amyloid fibrils found in patients suffering from either familial amyloidotic polyneuropathy or senile systemic amyloidosis. Familial amyloidotic polyneuropathy is an autosomal dominant hereditary type of amyloidosis which involves transthyretin with either one or two amino acid substitutions. The three-dimensional structure of chicken transthyretin was determined in order to compare a non-amyloidogenic, species-variant transthyretin with wild-type and mutant transthyretin molecules. Of the 31 chicken-to-human residue differences, 9 occur at positions which in human transthyretin give rise to amyloidogenic variants although none corresponds to the appropriate side-chain substitutions. The model of chicken transthyretin has been refined to an R-factor of 19.9%. The overall fold of the protein is that of an all-beta protein. Compared with wild-type human transthyretin the avian transthyretin shows quite large differences in the region known to be involved in binding to retinol-binding protein, it has a much shorter helical component than the human protein and some of the monomer-monomer interactions are different.
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__TOC__
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</StructureSection>
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==About this Structure==
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1TFP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TFP OCA].
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==Reference==
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The crystal structure of transthyretin from chicken., Sunde M, Richardson SJ, Chang L, Pettersson TM, Schreiber G, Blake CC, Eur J Biochem. 1996 Mar 1;236(2):491-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8612621 8612621]
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[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Blake, C C.F.]]
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[[Category: Blake CCF]]
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[[Category: Chang, L.]]
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[[Category: Chang L]]
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[[Category: Pettersson, T M.]]
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[[Category: Pettersson TM]]
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[[Category: Richardson, S J.]]
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[[Category: Richardson SJ]]
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[[Category: Schreiber, G.]]
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[[Category: Schreiber G]]
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[[Category: Sunde, M.]]
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[[Category: Sunde M]]
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[[Category: albumin]]
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[[Category: retinol-binding]]
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[[Category: transport (thyroxine)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:55:28 2008''
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Current revision

TRANSTHYRETIN (FORMERLY KNOWN AS PREALBUMIN)

PDB ID 1tfp

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