Michal Harel at 08:06, 30 December 2014

Michal Harel — Tue, 30 Dec 2014 08:06:16 GMT

←Older revision		Revision as of 08:06, 30 December 2014
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-	<Structure load='1gkc' size='400' frame='true' align='right' caption='MMP9' scene='Insert optional scene name here' />	+	<Structure load='1gkc' size='400' frame='true' align='right' caption='MMP9 complex with inhibitor, Ca+2 (green) and Zn+2 (grey) ions (PDB code [[1gkc]]).' scene='Insert optional scene name here' />

-	MMP9 is a member of ''' matrix metalloproteinases''' (MMPs) which are zinc-dependent endopeptidases. It has been found to associate with many types of cancers and investigated as a potential drug target. Various of <scene name='User:Jiaming_Zhuang/Sandbox_2/Ligand/1'>inhibitors</scene> have been designed to bind to the <scene name='User:Jiaming_Zhuang/Sandbox_2/Domain1/1'>catalytic domain</scene> and inhibit the activity of MMP9.	+	'''MMP9''' is a member of ''' matrix metalloproteinases''' (MMPs) which are zinc-dependent endopeptidases. It has been found to associate with many types of cancers and investigated as a potential drug target. Various of <scene name='User:Jiaming_Zhuang/Sandbox_2/Ligand/1'>inhibitors</scene> have been designed to bind to the <scene name='User:Jiaming_Zhuang/Sandbox_2/Domain1/1'>catalytic domain</scene> and inhibit the activity of MMP9.

Mallory Gordon: New page: MMP9 is a member of ''' matrix metalloproteinases''' (MMPs) which ar...

Mallory Gordon — Thu, 11 Dec 2014 01:04:38 GMT

New page: <Structure load='1gkc' size='400' frame='true' align='right' caption='MMP9' scene='Insert optional scene name here' /> MMP9 is a member of ''' matrix metalloproteinases''' (MMPs) which ar...

New page

<Structure load='1gkc' size='400' frame='true' align='right' caption='MMP9' scene='Insert optional scene name here' />

MMP9 is a member of ''' matrix metalloproteinases''' (MMPs) which are zinc-dependent endopeptidases. It has been found to associate with many types of cancers and investigated as a potential drug target. Various of <scene name='User:Jiaming_Zhuang/Sandbox_2/Ligand/1'>inhibitors</scene> have been designed to bind to the <scene name='User:Jiaming_Zhuang/Sandbox_2/Domain1/1'>catalytic domain</scene> and inhibit the activity of MMP9.

ProMMP9 has a propeptide domain with a zinc ligating "cysteine switch" at the <scene name='40/400553/Pro_cat_motif/4'>active site</scene>, rendering the enzyme inactive until the propeptide is cleaved.

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Reference:
Siân Rowsell, Paul Hawtin,Claire A. Minshull, Holly Jepson, Sarah M.V. Brockbank,Derek G. Barratt, Anthony M. Slater, William L. McPheat, David Waterson, Adriano M. Henney, Richard A. Pauptit Crystal Structure of Human MMP9 in Complex with a Reverse Hydroxamate Inhibitor, Volume 319, Issue 1, 24 May 2002, Pages 173–181
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Molecular Playground/MMP9 - Revision history

Michal Harel at 08:06, 30 December 2014

Mallory Gordon: New page: MMP9 is a member of ''' matrix metalloproteinases''' (MMPs) which ar...