EC Number   |
Protein Variants |
Reference |
|---|
   5.6.1.2 | DELTAkinA |
kinesin-1 mutant, has normal ATPase activity despite the absence of dynein plus-end accumulation |
712543 |
| 5.6.1.2 | E2022Q |
mutation in the Walker B motif of the AAA1 module. In the presence of ATP, the mutant is trapped in a single state, D*-ATP. It binds to microtubules with high affintiy, similar to wild-type |
689758 |
| 5.6.1.2 | E2488Q |
mutation in nucleotide-binding domain AAA3 |
698798 |
| 5.6.1.2 | E2819Q |
mutation in nucleotide-binding domain AAA4 |
698798 |
| 5.6.1.2 | K1975T |
Walker A mutation in the AAA1 module. Mutant tightly binds to microtubules in the presence and absence of ATP. The inhibition of ATP binding to the AAA1 ATPase site by the mutation completely blocks the ATP-induced dissociation of the complex with the microtubules |
689758 |
| 5.6.1.2 | K2675T |
Walker A mutation in the AAA1 module. Mutant tightly binds to microtubules in the presence and absence of ATP. Inhibition of ATP binding to the AAA3 ATPase site by the K2675T mutationdoes not block the ATP-induced dissociation of the complex with the microtubules |
689758 |
| 5.6.1.2 | L1098F |
mutation in the stem region of dynein heavy chain, suppression of the phenotype of nudF/lis1 loss |
686960 |
| 5.6.1.2 | L3339C/I3517C |
380-kDa motor domain mutant to introduce disulfide cross-linking |
700379 |
| 5.6.1.2 | L3339C/Q3510C |
380-kDa motor domain mutant to introduce disulfide cross-linking |
700379 |
| 5.6.1.2 | more |
expression of full-length two-headed heavy chain and of 380 kDa truncated single-head heavy chain. Four to five moelcules of single-headed heavy chain are required for continuous microtubule sliding, while one molecule of two-headed heavy chain is enough for sliding. The two heads of a single full-length dynein communicate with each other to take processive steps along a microtubule |
688691 |
