4B91
Crystal structure of truncated human CRMP-5
Summary for 4B91
| Entry DOI | 10.2210/pdb4b91/pdb |
| Related | 4B90 4B92 |
| Descriptor | DIHYDROPYRIMIDINASE-RELATED PROTEIN 5 (2 entities in total) |
| Functional Keywords | signaling protein, neurogenesis, phosphoprotein, crmp, tim barrel, axonal outgrowth, developmental protein |
| Biological source | HOMO SAPIENS (HUMAN) |
| Cellular location | Cytoplasm (Probable): Q9BPU6 |
| Total number of polymer chains | 2 |
| Total formula weight | 105906.99 |
| Authors | Ponnusamy, R.,Lohkamp, B. (deposition date: 2012-08-31, release date: 2013-02-13, Last modification date: 2023-12-20) |
| Primary citation | Ponnusamy, R.,Lohkamp, B. Insights Into the Oligomerization of Crmps: Crystal Structure of Human Collapsin Response Mediator Protein 5. J.Neurochem., 125:855-, 2013 Cited by PubMed Abstract: Collapsin response mediator protein-5 (CRMP-5) is the latest identified member of the CRMP cytosolic phosphoprotein family, which is crucial for neuronal development and repair. CRMPs exist as homo- and/or hetero-tetramers in vivo and participate in signaling transduction, cytoskeleton rearrangements, and endocytosis. CRMP-5 antagonizes many of the other CRMPs' functions either by directly interacting with them or by competing for their binding partners. We determined the crystal structures of a full length and a truncated version of human CRMP-5, both of which form a homo-tetramer similar to those observed in CRMP-1 and CRMP-2. However, solution studies indicate that CRMP-5 and CRMP-1 form weaker homo-tetramers compared with CRMP-2, and that divalent cations, Ca(2+) and Mg(2+), destabilize oligomers of CRMP-5 and CRMP-1, but promote CRMP-2 oligomerization. On the basis of comparative analysis of the CRMP-5 crystal structure, we identified residues that are crucial for determining the preference for hetero-oligomer or homo-oligomer formation. We also show that in spite of being the CRMP family member most closely related to dihydropyrimidinase, CRMP-5 does not have any detectable amidohydrolase activity. The presented findings provide new detailed insights into the structure, oligomerization, and regulation of CRMPs. PubMed: 23373749DOI: 10.1111/JNC.12188 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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