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English: MAD1 homodimer in unattached kinetochores is bound to two c-MAD2 and forms a catalytic receptor for cytozolic o-MAD2. Complex MAD1-cMAD2-oMAD2 catalyzes conformational change of inactive oMAD2 to the active c-MAD2 form. C-MAD2 then binds to Cdc20 and mediates APC/C inhibition and mitotic arrest.
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Author Cellular Biochemistry II

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10 April 2010

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Date/TimeThumbnailDimensionsUserComment
current17:42, 10 April 2010Thumbnail for version as of 17:42, 10 April 2010759 × 297 (25 KB)Cellular Biochemistry II{{Information |Description={{en|1=MAD1 homodimer in unattached kinetochores is bound to two c-MAD2 and forms a catalytic receptor for cytozolic o-MAD2. Complex MAD1-cMAD2-oMAD2 catalyzes conformational change of inactive oMAD2 to the active c-MAD2 form. C

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