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	==Quiz Question 1==		==Quiz Question 1==
-	<Structure load='3kgt' size='300' frame='true' align='right' caption='pdbcode, Insert caption here' scene='Insert optional scene name here' /> TTR has two identical thyroxine-binding sites located at the dimer-dimer interface. Locate them. It is the blue, green or grey/red structures? <scene name='48/483883/Quiz_1/3'>Tranthyretin</scene>	+	<Structure load='3kgt' size='300' frame='true' align='right' caption='pdbcode, Insert caption here' scene='Insert optional scene name here' />The substitution of a <scene name='48/483883/Quiz_1/5'>transthyretin</scene> hydrophobic side chain (maroon) for a hydrophilic side chain (blue) that is in the contact region between retinol binding protein and transthyretin results in:
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		+	A. An increase in binding affinity and increase in hydrophobic interactions.
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		+	B. A decrease or even complete loss of binding affinity.
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		+	C. No change in affinity, both polar and nonpolar interactions bind retinol-binding protein and transthyretin.
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		+	Answer:B
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Revision as of 21:11, 30 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 1 Human Transthyretin (TTR) complexed with genistein 2 Introduction 3 Overall Structure 4 Binding Interactions 5 Additional Features 6 Quiz Question 1 7 Quiz Question 2 8 See Also 9 Credits 10 References

Human Transthyretin (TTR) complexed with genistein

Introduction

spinqualitylabelsall models caption Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

1. Structure and characteristics of Transthyretin (TTR), where it can be found and its relevant concentration.

2. Function of TTR, what molecules it binds to and other responsibilities!

3. How TTR creates amorphous aggregates and/or amyloid fibrils.

4. Introduction of different amyloid diseases than can be created by the deposition of aggregates composed of variants of TTR.

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

spinqualitylabelsall models Front view along the bivalent hormone binding channel Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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 sandwich-like tertiary structure. The intermolecular contacts formed by the dimer–dimer interface result in the formation of a spacious channel (40 A ̊ long) running along the twofold symmetry axis of the protein. The channel is about 10 A ̊ wide at the outer rim and narrows in the centre to about 4 A ̊ . This narrowing is defined by the alignment of and on the bottom of the cleft.

Binding Interactions

spinqualitylabelsall models pdbcode, Insert caption here Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

As you can see, there are a total of five interactions. The Hydrogen Bonds are colored blue, and the hydrophobic interactions are colored pink. The orange color is where both hydrogen bonding and hydrophobic interactions occur at the same time.

Additional Features

spinqualitylabelsall models 3kgt, Insert caption here Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

-insert possible new starting green scene

-the binding of substrate to Transthyretin requires four TTR proteins to be bound to each other simultaneously.

-four-protein unit (tetramer)

-binding and transport of thyroxine and retinol requires tetramer

-retinol requires retinol binding protein

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Quiz Question 1

spinqualitylabelsall models pdbcode, Insert caption here Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

The substitution of a hydrophobic side chain (maroon) for a hydrophilic side chain (blue) that is in the contact region between retinol binding protein and transthyretin results in:

A. An increase in binding affinity and increase in hydrophobic interactions.

B. A decrease or even complete loss of binding affinity.

C. No change in affinity, both polar and nonpolar interactions bind retinol-binding protein and transthyretin.

Answer:B

Quiz Question 2

spinqualitylabelsall models pdbcode, Insert caption here Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

See Also

• 1dvq
• 1dvx
• 1bmz
• 4pm1
• 1bm7
• 1e4h
• 3cft

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

References