Sandbox Reserved 1125: Difference between revisions
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=== Endogenous inhibitors === | === Endogenous inhibitors === | ||
The tissue inhibitors of metalloproteinases (TIMPs) are | <Structure load='1UEA' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /> | ||
The tissue inhibitors of metalloproteinases (TIMPs) are specific inhibitors of the whole family of MMPs proteins. Currently, four TIMPs were identified (TIMP-1, TIMP-2, TIMP-3, TIMP-4). | |||
They are 21 to 29kDa proteins, contain 2 subdomains (N-ter and C-ter) and have a "wedge-like" shape. | |||
This is the N-ter domain which interacts with the catalytic domains of MMPs and impedes their proteolytic activity. | |||
The <scene name='71/719866/Timp1/1'>Cys1 residue</scene> is crucial for the inhibitor effect of TIMPs because it can interact with the catalytic zinc of the MMPs. The result is a chelation of the zinc by the N-terminal amino group and the carbonyl group of Cys1.[http://cardiovascres.oxfordjournals.org/content/69/3/562] | |||
=== Synthetic inhibitors === | === Synthetic inhibitors === | ||
