Structure and Functional Role of Dynein's Microtubule-Binding Domain
| Autor: | Joan E. Garbarino, Ronald A. Milligan, Ronald D. Vale, Wesley E. Shipley, Andrew P. Carter, Carol Cho, Elizabeth M. Wilson-Kubalek, I. R. Gibbons |
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| Rok vydání: | 2008 |
| Předmět: |
Models
Molecular Protein Folding Movement Recombinant Fusion Proteins Molecular Sequence Data Dynein macromolecular substances Flagellum Biology Crystallography X-Ray Microtubules Protein Structure Secondary Article Mice Adenosine Triphosphate Microtubule Dynein ATPase Image Processing Computer-Assisted Animals Amino Acid Sequence Cytoskeleton Coiled coil Binding Sites Multidisciplinary Cilium Dyneins Protein Structure Tertiary Microscopy Electron Protein Subunits Biochemistry Biophysics Crystallization Dimerization Hydrophobic and Hydrophilic Interactions Binding domain |
| Zdroj: | Science. 322:1691-1695 |
| ISSN: | 1095-9203 0036-8075 |
| Popis: | Dynein motors move various cargos along microtubules within the cytoplasm and power the beating of cilia and flagella. An unusual feature of dynein is that its microtubule-binding domain (MTBD) is separated from its ring-shaped AAA+ adenosine triphosphatase (ATPase) domain by a 15-nanometer coiled-coil stalk. We report the crystal structure of the mouse cytoplasmic dynein MTBD and a portion of the coiled coil, which supports a mechanism by which the ATPase domain and MTBD may communicate through a shift in the heptad registry of the coiled coil. Surprisingly, functional data suggest that the MTBD, and not the ATPase domain, is the main determinant of the direction of dynein motility. |
| Databáze: | OpenAIRE |
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