4B90

Crystal structure of WT human CRMP-5

Summary for 4B90

• Entry DOI: 10.2210/pdb4b90/pdb
• Related: 4B91 4B92
• Descriptor: DIHYDROPYRIMIDINASE-RELATED PROTEIN 5, 1,2-ETHANEDIOL (3 entities in total)
• Functional Keywords: signaling protein, neurogenesis, axonal outgrowth, developmental protein
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Cytoplasm (Probable): Q9BPU6
• Total number of polymer chains: 2
• Total formula weight: 128248.15

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

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: 23373749
DOI: 10.1111/JNC.12188

Experimental method

X-RAY DIFFRACTION (2.2 Å)