User:Genevieve Abbruzzese/Sandbox 1
From Proteopedia
(Difference between revisions)
| Line 8: | Line 8: | ||
| - | + | <applet size='[450,338]' frame='true' align='right' | |
| + | caption='ADAM13 homology model' /> | ||
<scene name='User:Genevieve_Abbruzzese/Sandbox_1/Adam13homologymodel/1'>TextToBeDisplayed</scene> | <scene name='User:Genevieve_Abbruzzese/Sandbox_1/Adam13homologymodel/1'>TextToBeDisplayed</scene> | ||
Revision as of 04:10, 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).
