6YPE
Crystal structure of the human neuronal pentraxin 1 (NP1) pentraxin (PTX) domain.
Summary for 6YPE
| Entry DOI | 10.2210/pdb6ype/pdb |
| Descriptor | Neuronal pentraxin-1, CALCIUM ION, CACODYLATE ION, ... (4 entities in total) |
| Functional Keywords | cell adhesion, synapse formation, ampa receptor |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 2 |
| Total formula weight | 45833.70 |
| Authors | Elegheert, J.,Clayton, A.J.,Aricescu, A.R. (deposition date: 2020-04-15, release date: 2020-06-03, Last modification date: 2024-10-09) |
| Primary citation | Suzuki, K.,Elegheert, J.,Song, I.,Sasakura, H.,Senkov, O.,Matsuda, K.,Kakegawa, W.,Clayton, A.J.,Chang, V.T.,Ferrer-Ferrer, M.,Miura, E.,Kaushik, R.,Ikeno, M.,Morioka, Y.,Takeuchi, Y.,Shimada, T.,Otsuka, S.,Stoyanov, S.,Watanabe, M.,Takeuchi, K.,Dityatev, A.,Aricescu, A.R.,Yuzaki, M. A synthetic synaptic organizer protein restores glutamatergic neuronal circuits. Science, 369:-, 2020 Cited by PubMed Abstract: Neuronal synapses undergo structural and functional changes throughout life, which are essential for nervous system physiology. However, these changes may also perturb the excitatory-inhibitory neurotransmission balance and trigger neuropsychiatric and neurological disorders. Molecular tools to restore this balance are highly desirable. Here, we designed and characterized CPTX, a synthetic synaptic organizer combining structural elements from cerebellin-1 and neuronal pentraxin-1. CPTX can interact with presynaptic neurexins and postsynaptic AMPA-type ionotropic glutamate receptors and induced the formation of excitatory synapses both in vitro and in vivo. CPTX restored synaptic functions, motor coordination, spatial and contextual memories, and locomotion in mouse models for cerebellar ataxia, Alzheimer's disease, and spinal cord injury, respectively. Thus, CPTX represents a prototype for structure-guided biologics that can efficiently repair or remodel neuronal circuits. PubMed: 32855309DOI: 10.1126/science.abb4853 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.45 Å) |
Structure validation
Download full validation report
