User:Genevieve Abbruzzese/Sandbox 1
From Proteopedia
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One of the [[CBI Molecules]] being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground]. | One of the [[CBI Molecules]] being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground]. | ||
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| + | <scene name='User:Genevieve_Abbruzzese/A13mdce/4'>ADAM13 modeled against ADAM22</scene> | ||
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ADAM13 is a transmembrane protein containing a metalloprotease (gray) and controls cell motility by shedding adhesion molecules from the cell surface. ADAM13 also exhibits adhesive activity through it's disintegrin (blue) and cysteine rich (purple) domains (EGF-like repeat, cyan). | ADAM13 is a transmembrane protein containing a metalloprotease (gray) and controls cell motility by shedding adhesion molecules from the cell surface. ADAM13 also exhibits adhesive activity through it's disintegrin (blue) and cysteine rich (purple) domains (EGF-like repeat, cyan). | ||
Revision as of 03:59, 10 December 2010
- User:Genevieve Abbruzzese/Sandbox 1
One of the CBI Molecules being studied in the University of Massachusetts Amherst Chemistry-Biology Interface Program at UMass Amherst and on display at the Molecular Playground.
ADAM13 is a transmembrane protein containing a metalloprotease (gray) and controls cell motility by shedding adhesion molecules from the cell surface. ADAM13 also exhibits adhesive activity through it's disintegrin (blue) and cysteine rich (purple) domains (EGF-like repeat, cyan).
Metalloprotease domain
Most ADAMs contain a canonical metalloprotease site (HExxHxxGxxH) with a catalytic glutamate residue (shown in red) three Histidine residues (blue) coordinating a Zinc ion (green).
<applet size='[450,338]' frame='true' align='left'
caption='Metalloprotease Active Site'
