Molecular Playground/ADAM13: Difference between revisions

New page: 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...
 
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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].
 
 
 
'''ADAM13''' is 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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<applet size='[450,338]' frame='true' align='right'
<applet size='[450,338]' frame='true' align='right'
caption='ADAM13 homology model' />
scene='User:Genevieve_Abbruzzese/Sandbox_1/Adam13homologymodel/1'
<scene name='User:Genevieve_Abbruzzese/Sandbox_1/Adam13homologymodel/1'>ADAM13 modeled against ADAM22</scene>
caption='ADAM13 homology model against ADAM22 [[3g5c]]' />
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 
 




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Molecular Playground banner: ADAM13 reduces cell adhesion to promotes cell motility.








Molecular Playground banner: ADAM13 reduces cell adhesion to promotes cell motility.




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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). ADAMs are known to cleave a variety of proteins present at the cell surface in addition to cell adhesion molecules, such as signaling receptors and their ligands to either activate or inactivate the signaling pathway. The Alfandari Lab currently studies the role of the meltrin subfamily of ADAMs in early embryo development.
Most ADAMs contain the canonical metalloprotease active site sequence (HExxHxxGxxH) with a catalytic glutamate residue (shown below in red) three Histidine residues (blue) that coordinate a zinc ion (green). In addition to cell adhesion molecules, ADAMs are known to cleave a variety of other biologically important proteins present at the cell surface, such as signaling receptors and their ligands to either activate or inactivate multiple signaling pathways. The [http://www-unix.oit.umass.edu/%7Ealfandar/ Alfandari Lab] currently studies the role of the meltrin subfamily of ADAMs in early embryo development.




[[Image:ADAM33metallo.png]]
[[Image:ADAM33metallo.png]]
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[[Category: Molecular Playground]]

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Genevieve Abbruzzese, Michal Harel