tailieunhanh - Báo cáo khoa học: Crystal and solution structure, stability and post-translational modifications of collapsin response mediator protein 2

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. | ỊFEBS Journal Crystal and solution structure stability and post-translational modifications of collapsin response mediator protein 2 Viivi Majava1 Noora Loytynoja1 Wei-Qiang Chen2 Gert Lubec2 and Petri Kursula1 1 Department of Biochemistry University of Oulu Finland 2 Department of Pediatrics MedicalUniversity of Vienna Austria Keywords divalent cations nervous system oligomeric status protein structure small-angle X-ray scattering Correspondence P. Kursula Department of Biochemistry University of Oulu . Box 3000 FIN-90014 Oulu Finland Fax 358 8 5531141 Tel 358 44 5658288 E-mail Database The coordinates and structure factors have been deposited in the Protein Data Bank under the accession code 2VM8 Received 28 April2008 revised 14 July 2008 accepted 17 July 2008 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 b-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 A 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. doi .

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