User:Genevieve Abbruzzese/Sandbox 1
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
*[[User:Genevieve Abbruzzese/Sandbox 1]] | *[[User:Genevieve Abbruzzese/Sandbox 1]] | ||
| + | |||
| + | |||
<applet size='[450,338]' frame='true' align='right' | <applet size='[450,338]' frame='true' align='right' | ||
caption='ADAM13 homology model' | caption='ADAM13 homology model' | ||
| Line 8: | Line 10: | ||
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). | ||
| + | |||
| + | |||
| + | |||
| + | |||
| + | |||
| + | |||
=== Metalloprotease domain === | === 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). | 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' | ||
[[Image:ADAM33metallo.png]] | [[Image:ADAM33metallo.png]] | ||
Revision as of 03:58, 10 December 2010
- User:Genevieve Abbruzzese/Sandbox 1
| |||||||||||
