Structure and Functional Role of Dynein's Microtubule-Binding Domain

• Published in: Science (American Association for the Advancement of Science) Vol. 322; no. 5908; pp. 1691 - 1695
• Main Authors: Carter, Andrew P, Garbarino, Joan E, Wilson-Kubalek, Elizabeth M, Shipley, Wesley E, Cho, Carol, Milligan, Ronald A, Vale, Ronald D, Gibbons, I.R
• Format: Journal Article
• Language: English
• Published: Washington, DC American Association for the Advancement of Science 12.12.2008; The American Association for the Advancement of Science
• Subjects: Adenosine triphosphatase; Adenosine triphosphatases; Adenosine Triphosphate - metabolism; Amino Acid Sequence; Analytical, structural and metabolic biochemistry; Animals; Binding and carrier proteins; Binding Sites; Biological and medical sciences; Biophysics; Cellular biology; Crystal structure; Crystallization; Crystallography, X-Ray; Crystals; Dimerization; Dimers; Dyneins - chemistry; Dyneins - metabolism; Freight; Fundamental and applied biological sciences. Psychology; Hydrophobic and Hydrophilic Interactions; Image Processing, Computer-Assisted; Mice; Microscopy, Electron; Microtubules; Microtubules - metabolism; Microtubules - ultrastructure; Modeling; Models, Molecular; Molecular biology; Molecular Sequence Data; Movement; Musical register; Protein Structure, Secondary; Protein Structure, Tertiary; Proteins; Recombinant Fusion Proteins - chemistry; Recombinant Fusion Proteins - metabolism; Rodents; Rotation; Motility; Enzyme; Rodentia; Dynein ATPase; Structure function relationship; Vertebrata; Mammalia; Mouse; Cytoskeleton; Hydrolases; Microtubule; Molecular domain; Cytoplasm; Crystalline structure

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-c...