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High-resolution model of the microtubule

Academic Article
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Overview

authors

  • Nogales, E.
  • Whittaker, M.
  • Milligan, Ronald
  • Downing, K. H.

publication date

  • January 1999

journal

  • Cell  Journal

abstract

  • A high-resolution model of the microtubule has been obtained by docking the crystal structure of tubulin into a 20 A 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.

subject areas

  • Crystallography, X-Ray
  • Microtubules
  • Models, Molecular
  • Protein Conformation
  • Tubulin
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Identity

International Standard Serial Number (ISSN)

  • 0092-8674

Digital Object Identifier (DOI)

  • 10.1016/s0092-8674(00)80961-7

PubMed ID

  • 9989499
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Additional Document Info

start page

  • 79

end page

  • 88

volume

  • 96

issue

  • 1

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