The Specificity of TIMP-2 for Matrix Metalloproteinases Can Be Modified by Single Amino Acid Mutations

Abstract excerpt

Residues 1-127 of human TIMP-2 (N-TIMP-2), comprising three of the disulfide-bonded loops of the TIMP-2 molecule, is a discrete protein domain that folds independently of the C-terminal domain. This domain has been shown to be necessary and sufficient for metalloproteinase inhibition and contains the major sites of interaction with the catalytic N-terminal domain of active matrix metalloproteinases (MMPs)....

Topics

Share this publication in a Topic to start or enrich a Post.

• Share to Peptidase Inhibition and Analysis
• Share to Protease and Inhibitor Mechanisms
• Share to Signaling Pathways in Disease