Sandbox Reserved 432
From Proteopedia
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-results in a shift of the connecting loop when compared to latent antithrombin | -results in a shift of the connecting loop when compared to latent antithrombin | ||
-Successfully inhibits antithrombin polymerisation | -Successfully inhibits antithrombin polymerisation | ||
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| + | <scene name='Sandbox_Reserved_432/Binding_site/1'>WMDF Binding Site</scene> | ||
===Additional Features=== | ===Additional Features=== | ||
Revision as of 14:47, 5 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 |
YourMacromolecule
Introduction
|
Overall Structure
Binding Interactions
WMDF - tetra peptide with bulky side chains
WMDF binds to P14-8 peptide-antithrombin binary complex
-Tetra peptide occupies P7-P4 vacancy -Forms 8 hydrogen bonds with adjacent residues
Methionine is at the P6 location, while phenylalanine is at P4 location
-P4 & P6 locations are very critical
-Hydrophobicity of P4 & P6 are consistent feature of effective serpin-derived peptides
-results in a shift of the connecting loop when compared to latent antithrombin
-Successfully inhibits antithrombin polymerisation
Additional Features
Credits
Introduction - Kevin Dillon
Overall Structure - Max Nowak
Drug Binding Site - Kyle Reed
Additional Features - Chris Carr
