Transthyretin

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{{STRUCTURE_1rlb| PDB=1rlb | SIZE=400| SCENE= |right|CAPTION=Transthyretin tetramer (grey, green, pink, yellow) complex with retinol-binding protein (cyan, magenta) and retinoic acid, [[1rlb]] }}
{{STRUCTURE_1rlb| PDB=1rlb | SIZE=400| SCENE= |right|CAPTION=Transthyretin tetramer (grey, green, pink, yellow) complex with retinol-binding protein (cyan, magenta) and retinoic acid, [[1rlb]] }}
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== Function ==
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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. TTR is known to be associated with amyloid diseases. For details see [[Student Project 2 for UMass Chemistry 423 Spring 2015]].
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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 [[Student Project 2 for UMass Chemistry 423 Spring 2015]].
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== Disease ==
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TTR mutations are associated with amyloid deposition<ref>PMID:7599630</ref>.
==3D structures of transthyretin==
==3D structures of transthyretin==
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**[[1sn5]] – gsTTR + T4 derivative
**[[1sn5]] – gsTTR + T4 derivative
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== References ==
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<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Revision as of 10:35, 21 September 2016

Template:STRUCTURE 1rlb

Contents

Function

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[1]. For details see Student Project 2 for UMass Chemistry 423 Spring 2015.

Disease

TTR mutations are associated with amyloid deposition[2].

3D structures of transthyretin

Updated on 21-September-2016

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

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

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