Transthyretin

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{{STRUCTURE_1rlb| PDB=1rlb | SIZE=400| SCENE= |right|CAPTION=Transthyretin complex with retinol-binding protein and retinoic acid, [[1rlb]] }}
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<StructureSection load='1tha' size='350' side='right' caption='Human transthyretin complex with tyroxine derivative [[1tha]]' scene='' pspeed='8'>
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== Function ==
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'''Transthyretin''' (TTR) is a serum carrier ot the thyroid hormone thyroxine (T4) and retinol through its association with retinol-binding protein (RBP). Many small molecules bind to TTR T4-binding site. TTR is known to be associated with amyloid diseases.
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'''Transthyretin''' (TTR) is a serum carrier of the thyroid hormone thyroxine (T4) and retinol through its association with retinol-binding protein (RBP). Many small molecules bind to TTR T4-binding site<ref>PMID:12553418</ref>. For details see [[Tafamidis]] and [[Student Project 2 for UMass Chemistry 423 Spring 2015]].
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{{TOC limit|limit=2}}
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== Disease ==
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TTR mutations are associated with amyloid deposition<ref>PMID:7599630</ref>. [[Tafamidis]] is a medication which stabilises TTR and is used in treatment of TTR amyloidosis<ref>PMID:30145929</ref>.
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== Structural highlights ==
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<scene name='46/466524/Cv/3'>The hormone tyrosine is bound in the active site of TTR</scene><ref>PMID:1730601</ref>.
==3D structures of transthyretin==
==3D structures of transthyretin==
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[[Transthyretin 3D structures]]
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[[2pab]], [[1tta]], [[1ttb]], [[1etb]], [[1bmz]], [[1f41]], [[1dvq]], [[1fh2]], [[1qwh]], [[2h4e]], [[2qgb]], [[3cbr]], [[3d7p]], [[3cfm]], [[3i9p]], [[3a4d]], [[3a4e]], [[3a4f]] – hTTR – human
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</StructureSection>
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[[1eta]], [[1ttc]], [[1tsh]], [[2trh]], [[2try]], [[1bzd]], [[1bze]], [[1fhn]], [[1g10]], [[1x7s]], [[2qel]], [[3dgd]], [[3did]], [[3kgs]] – hTTR (amyloidogenic mutant)
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[[1ttr]] – hTTR (cardiomyapatic mutant)
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[[1bz8]], [[5ttr]], [[1f86]], [[1gko]], [[1iii]], [[1iik]], [[1ijn]], [[1sok]], [[1soq]], [[1x7t]], [[2g3x]], [[2g3z]], [[2g4e]], [[2g4g]], [[2noy]], [[3bt0]], [[3cxf]], [[3djr]], [[3djs]], [[3djt]], [[3djz]], [[3dk0]], [[3dk2]], [[3do4]], [[3gps]], [[3grb]], [[3grg]], [[3i9a]], [[3i9i]] – hTTR (mutant)
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[[1tfp]] – TTR – chicken
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[[2qpf]] – TTR - mouse
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[[1oo2]], [[1sn2]] – gsTTR – gilthead seabream
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[[1gke]] – rTTR – rat
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'''TTR binary complexes'''
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[[1thc]], [[2h1x]], [[2h6u]] – hTTR + hydroxyaurone derivative
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[[1tlm]] – hTTR + milrinone
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[[1bm7]] – hTTR + flufenamic acid
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[[1dvs]], [[1dvt]], [[1dvu]], [[1dvx]], [[1dvy]], [[1dvz]], [[1tt6]], [[1tz8]], [[2f8i]], [[2fbr, [[2flm, [[2g5u]], [[2g9k]], [[2gab]], [[2qgc]], [[2qgd]], [[2qge]], [[3cn0]], [[3cn1]], [[3cn2]], [[3cn3]], [[3cn4]], [[3esn]], [[3eso]], [[3esp]], [[3glz]], [[3gs0]], [[3gs4]], [[3gs7]], [[3imr]], [[3ims]], [[3imt]], [[3imu]], [[3imv]], [[3imw]], [[3ipb]], [[3ipe]], [[3m10]] – hTTR + amyloid disease inhibitor
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[[1u21]], [[3cfn]], [[3cfq]], [[3cft]], [[3hj0]], [[3nee]], [[3neo]], [[3p3r]], [[3p3s]], [[3p3t]], [[3p3u]] – hTTR + inhibitor
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[[1e3f]], [[1e4h]], [[1e5a]], [[2b15]] – hTTR + phenol derivative
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[[2b14]], [[2b16]] – hTTR (mutant) + phenol derivative
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[[3kgt]], [[3kgu]] – hTTR (mutant) + genistein
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[[3ng5]] – hTTR (mutant) + epigallocatechin gallate
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[[3nes]], [[3nex]] – hTTR (mutant) + inhibitor
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[[1tyr]] – hTTR + retinoic acid
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[[1kgi]] – rTTR + tetraiodotyroacetic acid
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[[1z7t]] - hTTR + tetraiodotyroacetic acid
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[[1kgj]] – rTTR + dibromoflavone
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[[1zcr]], [[1zd6]] – hTTR + anion
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[[1y1d]], [[2b77]], [[2b9a]], [[3d2t]], [[3fc8]], [[3fcb]] – hTTR + diflunisal derivative
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[[3b56]] – hTTR + salicylic acid derivative
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'''TTR complexes with retinol-binding protein'''
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[[1rlb]], [[1qab]] – hTTR + RBP
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[[2wqa]] – hTTR + RBP + oleic acid
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[[3bsz]] – hTTR + RBP + antibody
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'''TTR complexes with thyroxine'''
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[[2rox]], [[1ict]] – hTTR + T4
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[[3ozk]] – hTTR (mutant) + T4
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[[1tha]], [[2roy]] – hTTR + T4 derivative
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[[1ie4]] – rTTR + T4
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[[1sn0]] – gsTTR + T4
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[[1sn5]] – gsTTR + T4 derivative
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== References ==
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<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

Human transthyretin complex with tyroxine derivative 1tha

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References

  1. ↑ Robbins J. Transthyretin from discovery to now. Clin Chem Lab Med. 2002 Dec;40(12):1183-90. PMID:12553418 doi:http://dx.doi.org/10.1515/CCLM.2002.208
  2. ↑ Saraiva MJ. Transthyretin mutations in health and disease. Hum Mutat. 1995;5(3):191-6. PMID:7599630 doi:http://dx.doi.org/10.1002/humu.1380050302
  3. ↑ Maurer MS, Schwartz JH, Gundapaneni B, Elliott PM, Merlini G, Waddington-Cruz M, Kristen AV, Grogan M, Witteles R, Damy T, Drachman BM, Shah SJ, Hanna M, Judge DP, Barsdorf AI, Huber P, Patterson TA, Riley S, Schumacher J, Stewart M, Sultan MB, Rapezzi C. Tafamidis Treatment for Patients with Transthyretin Amyloid Cardiomyopathy. N Engl J Med. 2018 Sep 13;379(11):1007-1016. PMID:30145929 doi:10.1056/NEJMoa1805689
  4. ↑ Wojtczak A, Luft J, Cody V. Mechanism of molecular recognition. Structural aspects of 3,3'-diiodo-L-thyronine binding to human serum transthyretin. J Biol Chem. 1992 Jan 5;267(1):353-7. PMID:1730601

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

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