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High-resolution model of the microtubule
Author(s): Nogales E, Whittaker M, Milligan RA, Downing KH
Source: CELL    Volume: 96    Issue: 1    Pages: 79-88    Published: JAN 8 1999  
Times Cited: 468     References: 42     
Abstract: A high-resolution model of the microtubule has been obtained by docking the crystal structure of tubulin into a 20 Angstrom map of the microtubule. The excellent fit indicates the similarity of the tubulin conformation in both polymers and defines the orientation of the tubulin structure within the microtubule. Long C-terminal helices form the crest on the outside of the protofilament, while long loops define the microtubule lumen. The exchangeable nucleotide in beta-tubulin is exposed at the plus end of the microtubule, while the proposed catalytic residue in alpha-tubulin is exposed at the minus end. Extensive longitudinal interfaces between monomers have polar and hydrophobic components. At the lateral contacts, a nucleotide-sensitive helix interacts with a loop that contributes to the binding site of taxol in beta-tubulin.
Document Type: Article
Language: English
Reprint Address: Nogales, E (reprint author), Univ Calif Berkeley, Lawrence Berkeley Lab, Berkeley, CA 94720 USA
Addresses:
1. Univ Calif Berkeley, Lawrence Berkeley Lab, Berkeley, CA 94720 USA
2. Univ Calif Berkeley, Dept Mol & Cell Biol, Berkeley, CA 94720 USA
3. Scripps Res Inst, Dept Cell Biol, La Jolla, CA 92037 USA
Publisher: CELL PRESS, 1050 MASSACHUSETTES AVE, CIRCULATION DEPT, CAMBRIDGE, MA 02138 USA
Subject Category: Biochemistry & Molecular Biology; Cell Biology
IDS Number: 156VR
ISSN: 0092-8674
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