File:MAD1 function in SAC.jpg
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Summary
| Description |
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. |
| Date | |
| Source | Own work |
| Author | Cellular Biochemistry II |
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| Date/Time | Thumbnail | Dimensions | User | Comment | |
|---|---|---|---|---|---|
| current | 17:42, 10 April 2010 | | 759 × 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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