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|2vm8, resolution 1.90Å ()|
HUMAN CRMP-2 CRYSTALLISED IN THE PRESENCE OF MG
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 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.
Crystal and solution structure, stability and post-translational modifications of collapsin response mediator protein 2., Majava V, Loytynoja N, Chen WQ, Lubec G, Kursula P, FEBS J. 2008 Sep;275(18):4583-96. Epub 2008 Aug 11. PMID:18699782
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.