期刊
FEBS JOURNAL
卷 275, 期 18, 页码 4583-4596出版社
WILEY
DOI: 10.1111/j.1742-4658.2008.06601.x
关键词
divalent cations; nervous system; oligomeric status; protein structure; small-angle X-ray scattering
资金
- Finnish MS Foundation
- Department of Biochemistry, Oulu University
- European Community Research Infrastructure Action
- [RII3-CT-2004-506008 (IA-SFS)]
The collapsin response mediator protein 2 (CRMP-2) is a central molecule regulating axonal growth cone guidance. It interacts with the cytoskeleton and mediates signals related to myelin-induced axonal growth inhibition. CRMP-2 has also been characterized as a constituent of neurofibrillary tangles in Alzheimer's disease. CD spectroscopy and thermal stability assays using the Thermofluor method indicated that Ca2+ and Mg2+ affect the stability of CRMP-2 and prevent the formation of beta-aggregates upon heating. Gel filtration showed that the presence of Ca2+ or Mg2+ promoted the formation of CRMP-2 homotetramers, and this was further proven by small-angle X-ray scattering experiments, where a 3D solution structure for CRMP-2 was obtained. Previously, we described a crystal structure of human CRMP-2 complexed with calcium. In the present study, we determined the structure of CRMP-2 in the absence of calcium at 1.9 angstrom resolution. When Ca2+ was omitted, crystals could only be grown in the presence of Mg2+ ions. By a proteomic approach, we further identified a number of post-translational modifications in CRMP-2 from rat brain hippocampus and mapped them onto the crystal structure.
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