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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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 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 [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]] | ||