The 4 Å X-ray structure of a tubulin: Stathmin-like domain complex

Cell

Volumn 102, Issue 6, 2000, Pages 809-816

  Gigant, Benoît ^a   Curmi, Patrick A ^b   Martin Barbey, Carole ^a   Charbaut, Elodie ^b   Lachkar, Sylvie ^b   Lebeau, Luc ^c   Siavoshian, Samila ^a,b   Sobel, André ^b   Knossow, Marcel ^a  

^a LABORATOIRE D ENZYMOLOGIE ET BIOCHIMIE STRUCTURALES   (France)

^b INSTITUT DU FER À MOULIN   (France)

^c UNIVERSITÉ DE STRASBOURG   (France)

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN SUBUNIT; STATHMIN; TUBULIN; MICROTUBULE PROTEIN; PHOSPHOPROTEIN;

ALPHA HELIX; AMINO ACID SEQUENCE; ANIMAL TISSUE; ARTICLE; COMPLEX FORMATION; CONTROLLED STUDY; DEPOLYMERIZATION; MICROTUBULE; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN ASSEMBLY; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; ANIMAL; BINDING SITE; BRAIN LEVEL; CATTLE; CHEMISTRY; DIMERIZATION; ISOLATION AND PURIFICATION; METABOLISM; MOLECULAR GENETICS; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; X RAY CRYSTALLOGRAPHY;

ANIMALIA;

AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; BRAIN CHEMISTRY; CATTLE; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; MICROTUBULE PROTEINS; MICROTUBULES; MOLECULAR SEQUENCE DATA; PHOSPHOPROTEINS; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; STATHMIN; TUBULIN;

EID: 0034664244     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)00069-6     Document Type: Article

References (44)

1. Methods used in the structure determination of bovine mitochondrial F1 ATPase
2. Gapped BLAST and PSI-BLAST: A new generation of protein database search programs
3. Identification of in vitro phosphorylation sites in the growth cone protein SCG10. Effect of phosphorylation site mutants on microtubule-destabilizing activity
4. Identification of a protein that interacts with tubulin dimers and increases the catastrophe rate of microtubules
5. Crystallography and NMR system: A new software suite for macromolecular structure determination
6. The free energy of hydrolysis of a microtubule-bound nucleoside triphosphate is near zero: All of the free energy for hydrolysis is stored in the microtubule lattice
7. The CCP4 suite: Programs for protein crystallography
8. Molecular characterization of human stathmin expressed in Escherichia coli: Site-directed mutagenesis of two phosphorylatable serines (Ser-25 and Ser-63)
9. The stathmin tubulin interaction in vitro
10. Solution structure of GDP-tubulin double rings to 3 nm resolution and comparison with microtubules
11. Phosphorylation regulates the microtubule-destabilizing activity of stathmin and its interaction with tubulin
12. A single cDNA encodes two isoforms of stathmin, a developmentally regulated neuron-enriched phosphoprotein
13. An extensively modified version of MolScript that includes greatly enhanced coloring capabilities
14. The stathmin phosphoprotein family: Intracellular localization and effects on the microtubule network
15. Regulation of microtubule dynamics by extracellular signals: cAMP-dependent protein kinase switches off the activity of oncoprotein 18 in intact cells
16. N-myc gene amplification in neuroblastoma is associated with altered phosphorylation of a proliferation related polypeptide (Op 18)
17. The microtubule-destabilizing activity of metablastin (p19) is controlled by phosphorylation
18. Dissociation of the tubulin-sequestering and microtubule catastrophe-promoting activities of oncoprotein 18/stathmin
19. Improved methods for building protein models in electron density maps and the location of errors in these models
20. Stathmin is a tubulin sequestering protein which forms a ternary T2S complex with two tubulin molecules
21. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
22. Mutations of oncoprotein 18/stathmin identify tubulin-directed regulatory activities distinct from tubulin association
23. Microtubule dynamics and microtubule caps: A time-resolved cryo-electron microscopy study
24. Oncoprotein 18 is a phosphorylation-responsive regulator of microtubule dynamics
25. A single amino acid difference distinguishes the human and the rat sequences of stathmin, a ubiquitous intracellular phosphoprotein associated with cell regulations
26. The stathmin gene family: Phylogenetic conservation and developmental regulation in Xenopus
27. Regulation of microtubule dynamics by Ca2+/calmodulin-dependent kinase IV/Gr-dependent phosphorylation of oncoprotein 18
28. Cold depolymerization of microtubules to double rings: Geometric stabilization of assemblies
29. Dynamic instability of microtubule growth
30. Structural changes at microtubule ends accompanying GTP hydrolysis: Information from a slowly hydrolyzable analogue of GTP, guanylyl (α,β)methylenediphosphonate
31. AMoRe: An automated package for molecular replacement
32. On the fast translation functions for molecular replacement
33. Structure of the αβ tubulin dimer by electron crystallography
34. High-resolution model of the microtubule
35. Processing of x-ray diffraction data collected in oscillation mode
36. The stathmin family - Molecular and biological characterization of novel mammalian proteins expressed in the nervous system
37. Probing the native structure of stathmin and its interaction domains with tubulin
38. Torsion angle dynamics: Reduced variable conformational sampling enhances crystallographic structure refinement
39. Regulation of microtubule dynamics by the neuronal growth-associated protein SCG10
40. PHD-an automatic server for protein secondary structure prediction
41. Stathmin: A relay phosphoprotein for multiple signal transduction?
42. Intracellular substrates for extracellular signaling: Characterization of a ubiquitous, neuron-enriched phosphoprotein (stathmin)
43. Op18/stathmin caps a kinked protofilament-like tubulin tetramer
44. Model for stathmin/OP18 binding to tubulin