User:Genevieve Abbruzzese/Sandbox 1

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<scene name='User:Genevieve_Abbruzzese/A13mdce/4'>ADAM13 modeled against ADAM22</scene>
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<scene name='User:Genevieve_Abbruzzese/Sandbox_1/Adam13homologymodel/1'>TextToBeDisplayed</scene>

Revision as of 04:08, 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).


Image:ADAM33metallo.png

Proteopedia Page Contributors and Editors (what is this?)

Genevieve Abbruzzese

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