Sandbox Reserved 431
From Proteopedia
| 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
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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
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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
