Transthyretin

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
 
+
<StructureSection load='1tha' size='340' side='right' caption='Human transthyretin complex with tyroxine derivative [[1tha]]' scene=''>
-
<StructureSection load='1tha' size='340' side='right' caption='Human transthyretin tetramer (grey, green, pink, yellow) complex with retinol-binding protein (cyan, magenta) and tyroxine derivative [[1tha]]' scene=''>
+
== Function ==
== 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<ref>PMID:12553418</ref>. For details see [[Student Project 2 for UMass Chemistry 423 Spring 2015]].
'''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]].

Revision as of 08:00, 22 September 2016

Human transthyretin complex with tyroxine derivative 1tha

Drag the structure with the mouse to rotate

3D structures of transthyretin

Updated on 22-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
  3. 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

Personal tools