Preliminary crystallographic study of a complex formed between the alpha/beta-tubulin heterodimer and the neuronal growth-associated protein SCG10.
Crystals of a complex formed between the alpha/beta-tubulin heterodimer and SCG10, a neuron-specific growth-associated protein, have been obtained by the hanging drop method. They belong to the space group P2(1)2(1)2(1), with unit cell parameters a = 56 A, b = 353 A, c = 466 A and four molecular complexes in the asymmetric unit. A complete X-ray diffraction data set to 6.1 A resolution has been collected using synchrotron radiation. This represents a challenging opportunity to study at a molecular level the structure-function relationships between a microtubule-destabilizing protein, SCG10, and tubulin.
Fleury
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D
Institut de Biologie Structurale Jean-Pierre Ebel, CEA/CNRS/University Joseph Fourier, 41 rue Jules Horowitz, Grenoble Cedex 1, 38027, France.
Grenningloh
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G
Lafanechère
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L
Antonsson
B
B
Job
D
D
Cohen-Addad
C
C
D000818:Animals; D001921:Brain / Q000378:metabolism; D002417:Cattle; D003460:Crystallization; D019281:Dimerization; D046911:Macromolecular Substances; D009414:Nerve Growth Factors / Q000737:chemistry* / Q000378:metabolism*; D009419:Nerve Tissue Proteins / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding; D020836:Protein Structure, Quaternary; D014404:Tubulin / Q000737:chemistry* / Q000378:metabolism*; D014961:X-Ray Diffraction
D046911:Macromolecular Substances; D009414:Nerve Growth Factors; D009419:Nerve Tissue Proteins; D014404:Tubulin