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Literature summary for 5.6.1.4 extracted from
- A lever-arm rotation drives motility of the minus-end-directed kinesin Ncd (2006), Nature, 439, 875-878.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| upon ATP binding, a coiled-coil mechanical element of microtubule-bound Ncd rotates about 79° towards the minus end | Drosophila melanogaster |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | construction of a single-headed Ncd heterodimer in which one polypeptide consists of an intact Ncd catalytic core and neck (residues 280700) and the second polypeptide consists of the neck region alone (residues 281347). This motor elicits microtubule gliding at a velocity comparable to that of the normal twoheaded Ncd homodimer with a similar ATPase kcat-value | Drosophila melanogaster |
| N600K | mutant lacks directional preference. Mutant shows unstable nucleotide-dependent conformations of its coiled coil | Drosophila melanogaster |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Drosophila melanogaster | - |
isoform Ncd | - |
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