Children with Rare, Debilitating Brain Diseases Suffer From Mutations in a Little-Known Protein Complex (VIDEO)
Caption
This video shows how the tubulin cofactors regulate the formation of tubulin dimers. They first form a cage (State I) that latches onto the red β-tubulin protein (State II), preventing it from pairing up into ββ-tubulin dimers, which are toxic to cells. The peach-colored α-tubulin binds to the cage (State III) and is pulled into position beneath β-tubulin (State IV). A light green GTP molecule binds to the top end of the cage, flipping a molecular latch, which causes the entire cage to bend – triggering a series of motions that roll α-tubulin into tight contact with β-tubulin (States V and VI), forming the stable αβ-tubulin dimer (State IV) that is then released. The remainder for video shows the sequence of steps in which αβ dimers are separated.
Credit
Video by Al-Bassam Lab / UC Davis
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May be used with acknowledgement.
License
Original content