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== Caspase-7 Structure ==
== Caspase-7 Structure ==
[[Image:CASP7cleavagesites.jpg | thumb| Cleavage sites of caspase-7]]
[[Image:CASP7cleavagesites.jpg | thumb| Cleavage sites of caspase-7]]
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Caspases are crystallized as homodimers. As previously stated, the caspases undergo proteolytic cleavage by the initiator caspases to assume their active conformations. Some caspases undergo more cleave than others. For executioner caspase-7 there exists three major cleavage sites, D23, D198 and D207. D23 processing removes the pro domain from the large subunit, where as, D198 and D207 is the major cleavage site for processing and removal of the inter-subunit linker. Caspase-7 has one minor cleavage site also located within the inter-subunit linker at D192.
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Caspases are crystallized as homodimers. As previously stated, the caspases undergo proteolytic cleavage by the initiator caspases to assume their active conformations. Some caspases undergo more cleavage than others. Caspase-7 has three major cleavage sites: D23, D198 and D207. D23 processing removes the prodomain from the large subunit, whereas D198 and D207 are the major cleavage sites for processing and removal of the inter-subunit linker. Caspase-7 has one minor cleavage site also located within the inter-subunit linker at D192.

Revision as of 16:22, 3 December 2013

Caspases are a family of CBI Molecules being studied in the University of Massachusetts Amherst Chemistry-Biology Interface Program at UMass Amherst and on display at the Molecular Playground.

Executioner Caspase-7

Structure of caspase-7(PDB entry 1f1j)

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

Derek MacPherson, Maureen E. Hill

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