2VM8

Human CRMP-2 crystallised in the presence of Mg

Summary for 2VM8

• Entry DOI: 10.2210/pdb2vm8/pdb
• Related: 2GSE
• Descriptor: DIHYDROPYRIMIDINASE-RELATED PROTEIN 2, MAGNESIUM ION (3 entities in total)
• Functional Keywords: neurogenesis, phosphoprotein, differentiation, crmp, cytoplasm, tim barrel, polymorphism, axonal pathfinding, developmental protein, signaling protein
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Cytoplasm, cytosol : Q16555
• Total number of polymer chains: 4
• Total formula weight: 220460.79

Authors

Kursula, P. (deposition date: 2008-01-24, release date: 2008-08-26, Last modification date: 2023-12-13)

Primary citation

Majava, V.,Loytynoja, N.,Chen, W.Q.,Lubec, G.,Kursula, P.
Crystal and Solution Structure, Stability and Post- Translational Modifications of Collapsin Response Mediator Protein 2.
FEBS J., 275:4583-, 2008

PubMed Abstract: 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.

PubMed: 18699782
DOI: 10.1111/J.1742-4658.2008.06601.X

Experimental method

X-RAY DIFFRACTION (1.9 Å)