Sandbox Reserved 431

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(Overall Structure)
(Overall Structure)
Line 23: Line 23:
<br> Protein-tyrosine phosphatase - composed of 6 monomers
<br> Protein-tyrosine phosphatase - composed of 6 monomers
<br> Each monomer is composed of 283 amino acids
<br> Each monomer is composed of 283 amino acids
 +
 +
This is NOT the biological unit. Talk to me if you need help with this. Prof T
 +

Revision as of 20:18, 9 March 2012


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

Phosphatase Inhibitor complexes: pdb 1nny

Insert caption here

Drag the structure with the mouse to rotate

Introduction

→ Function: enzyme that decreases the amount of insulin receptor in the cell, which increases the effectiveness of the insulin produced in the body

→ Why important to diabetes: type 2 diabetes is caused by the inability to use insulin effectively. Since phosphatase inhibitors increase the effectiveness of insulin in the cell, it has proved effective in treating type 2 diabetes

→ Nonselective competitive inhibitor

→ Multiple ligand binding sites – inhibitor binds with catalytic site in “open” position. Proves competitive inhibition

→ Formed by being genetically manipulated

Overall Structure


Protein-tyrosine phosphatase - composed of 6 monomers
Each monomer is composed of 283 amino acids

This is NOT the biological unit. Talk to me if you need help with this. Prof T



The monomer has 2 β strands and 10 β sheets - some mixed and some antiparallel and 9 α helices

Binding Interactions

-This is a competitive inhibitor

-It has good selectivity over other phosphatases

-Ligand binds via 2 binding sites

-Binding is reversible


<

Additional Features

The two Arg residues depicted, Arg24 and Arg254, may participate in a salt bridge or a hydrogen bonding interaction with napthoic acid, thus providing a site 2 ligand.

Credits

Introduction - Jill Carlson

Overall Structure - Polina Berdnikova

Drug Binding Site - Brett Clinton

Additional Features - James Hamblin

References

Personal tools