Active site binding loop stabilization in the subtilisin inhibitor eglin c: structural and functional studies on specifically designed mutants in complex with subtilisin and the uncomplexed inhibitor.

Abstract excerpt

As known from the x-ray crystal structure in complex with a proteinase and from NMR studies, the serine proteinase inhibitor eglin c has a wedge-like shape with a hydrophobic core and a solvent exposed active site binding loop which is stabilized by a network of non-covalent core-binding loop int...

Topics

• Binding Sites
• Crystallography, X-Ray
• Drug Stability
• Mutation
• Protein Engineering
• Protein Structure, Secondary
• Proteins
• Serine Proteinase Inhibitors
• Serpins
• Structure-Activity Relationship
• Subtilisins