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Literature summary for 5.6.1.2 extracted from
- Dynein swings into action (2009), Cell, 136, 395-396.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| all dyneins share a conserved motor domain. The core of the dynein motor domain consists of six tandem AAA+ ATPase domains. The first AAA+ domain (AAA1) is the primary site of ATP hydrolysis, whereas the other five domains (AAA2-6) have regulatory or structural functions. The dynein linker domain acts as a relatively rigid lever that amplifies small conformational changes in the AAA+ domains upon ATP hydrolysis | Dictyostelium discoideum |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Dictyostelium discoideum | - |
- |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| dynein | - |
Dictyostelium discoideum |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | dynein acts as a motor protein and converts the energy stored in ATP into movement by coupling the cycle of ATP hydrolysis to structural changes in the motor protein. The dynein motor family is composed of several axonemal forms that drive the beating of cilia, flagella and two cytoplasmic forms that are responsible for a range of cellular functions such as cargo transport, mitosis, and cell polarization | Dictyostelium discoideum |
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Release 2023.1 (January 2023)
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