Structural Basis of Extracellular Matrix Interactions with Matrix Metalloproteinases

摘要: Interactions of the extracellular matrix (ECM) with domains metalloproteinases (MMPs) increase their proteolytic action upon components. This occurs by multiple structural means. The activating interactions a partner protein pro-MMP-9 and GAGs pro-MMP-7 were reported. fibrillar proteins catalytic can traverse breadth active site cleft overflow into neighboring exosite perhaps beyond. Exosite bear some resemblance to precedents in thrombin complexes. Basket-shaped surfaces on fibronectin II-like modules (inserted MMP-2 -9) appear bind fibrils, may bend them, certainly unwind triple helices. C-terminal hemopexin are joined loosely domain, which might facilitate positioning movement across collagen At least first blade β-propeller domain MMP-1 seems interact helix. Unifying themes among diverse MMPs ECM polymers (1) that two MMP often participate (2) interaction guides for action.