The 4 A X-ray Structure of a Tubulin:stathmin-Like Domain Complex

Cell. 2000 Sep 15;102(6):809-16. doi: 10.1016/s0092-8674(00)00069-6.

Abstract

Phosphoproteins of the stathmin family interact with the alphabeta tubulin heterodimer (tubulin) and hence interfere with microtubule dynamics. The structure of the complex of GDP-tubulin with the stathmin-like domain of the neural protein RB3 reveals a head-to-tail assembly of two tubulins with a 91-residue RB3 alpha helix in which each copy of an internal duplicated sequence interacts with a different tubulin. As a result of the relative orientations adopted by tubulins and by their alpha and beta subunits, the tubulin:RB3 complex forms a curved structure. The RB3 helix thus most likely prevents incorporation of tubulin into microtubules by holding it in an assembly with a curvature very similar to that of the depolymerization products of microtubules.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Brain Chemistry
  • Cattle
  • Crystallography, X-Ray
  • Dimerization
  • Microtubule Proteins*
  • Microtubules / chemistry
  • Molecular Sequence Data
  • Phosphoproteins / chemistry*
  • Phosphoproteins / isolation & purification
  • Phosphoproteins / metabolism
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Stathmin
  • Tubulin / chemistry*
  • Tubulin / isolation & purification
  • Tubulin / metabolism

Substances

  • Microtubule Proteins
  • Phosphoproteins
  • Stathmin
  • Tubulin

Associated data

  • PDB/1FFX