Sandbox Reserved 426
From Proteopedia
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| - | =='''Human Transthyretin (TTR)'''== | + | =='''Human Transthyretin (TTR) complexed with genistein '''== |
==Introduction== | ==Introduction== | ||
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==Overall Structure== | ==Overall Structure== | ||
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| + | Human transthyretin (TTR) is a 55 kDa homotetramer (or more precisely, a dimer of dimers) that transports thyroxine and retinol-binding protein in the blood and cerebrospinal fluid. The monomer consists of two four-stranded β-sheets, arranged in a <scene name='48/483883/Sandwitch/1'>sandwich-like</scene> tertiary structure. | ||
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Revision as of 00:56, 13 March 2015
| This Sandbox is Reserved from January 19, 2016, through August 31, 2016 for use for Proteopedia Team Projects by the class Chemistry 423 Biochemistry for Chemists taught by Lynmarie K Thompson at University of Massachusetts Amherst, USA. This reservation includes Sandbox Reserved 425 through Sandbox Reserved 439. |
Contents |
Human Transthyretin (TTR) complexed with genistein
Introduction
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Human Transthyretin (TTR) is a gene that provides instructions for the producing of a protein called transthyretin. Transthyretin is composed of identical 127-aa sandwich subunits (shown in pink) that are produced primarily in the liver.
Overall Structure
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Human transthyretin (TTR) is a 55 kDa homotetramer (or more precisely, a dimer of dimers) that transports thyroxine and retinol-binding protein in the blood and cerebrospinal fluid. The monomer consists of two four-stranded β-sheets, arranged in a tertiary structure.
Binding Interactions
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Additional Features
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Quiz Question 1
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Quiz Question 2
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See Also
Credits
Introduction - name of team member
Overall Structure - name of team member
Drug Binding Site - name of team member
Additional Features - name of team member
Quiz Question 1 - name of team member
Quiz Question 2 - name of team member

