Sandbox Reserved 1125: Difference between revisions
From Proteopedia
Jump to navigationJump to search
Laura Dutto (talk | contribs) No edit summary |
Laura Dutto (talk | contribs) No edit summary |
||
| Line 76: | Line 76: | ||
The Cys1 residue 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.<ref>PMID:16405877</ref> Moreover, this interaction triggers the expulsion of the water molecule which was bound to the zinc. | The Cys1 residue 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.<ref>PMID:16405877</ref> Moreover, this interaction triggers the expulsion of the water molecule which was bound to the zinc. | ||
No structures of MMP-8 with TIMPs are available on PDB. However, the mecanism of inhibition is common to all the MMPs. To see the interaction between the catalytic domain of MMP-3 and TIMP-1 (in green) click <scene name='71/719866/Timp1/4'>here</scene>.<ref> | No structures of MMP-8 with TIMPs are available on PDB. However, the mecanism of inhibition is common to all the MMPs. To see the interaction between the catalytic domain of MMP-3 and TIMP-1 (in green) click <scene name='71/719866/Timp1/4'>here</scene>.<ref>[http://www.rcsb.org/pdb/explore/explore.do?structureId=1UEA "Metalloprotease-Inhibitor Complex</ref> | ||
=== Synthetic inhibitors === | === Synthetic inhibitors === | ||
