1H, 13C, and 15N chemical shift assignment of human PACSIN1/syndapin I SH3 domain in solution - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue Biomolecular NMR Assignments Année : 2020

1H, 13C, and 15N chemical shift assignment of human PACSIN1/syndapin I SH3 domain in solution

Résumé

Human neuron-specific PACSIN1 plays a key role in synaptic vesicle recycling and endocytosis, as well as reorganization of the microtubule dynamics to maintain axonal plasticity. PACSIN1 contains a highly conserved C-terminal SH3 domain and an F-bar domain at its N-terminus. Due to its remarkable interaction network, PACSIN1 plays a central role in key neuronal functions. Here, we present a robust backbone and side-chain assignment of PACSIN1 SH3 domain based on 2D [1H,15N] HSQC or HMQC, and 3D BEST-HNCO, -HNCACB, -HN(CO)CACB, -HN(CA)CO, and standard (H)CC(CO)NH, HN(CA)NNH, HN(COCA)NH, HBHANNH, HNHA, HBHA(CO)NH, H(CC)(CO)NH, HCCH-TOCSY, that covers 96% for all 13CO, 13Cα and 13Cβ, 28% of 13Cγδε, and 95% of 1HN and 15N chemical shifts. Modelling based on sequence homology with a known related structure, and chemical shift-based secondary structure predictions, identified the presence of five β-strands linked by flexible loops. Taken together, these results open up new avenues to investigate and develop new therapeutic strategies.
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Dates et versions

hal-02537946 , version 1 (10-04-2020)

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Emmanuelle Boll, François-Xavier Cantrelle, Isabelle Landrieu, Matthieu Hirel, Davy Sinnaeve, et al.. 1H, 13C, and 15N chemical shift assignment of human PACSIN1/syndapin I SH3 domain in solution. Biomolecular NMR Assignments, 2020, ⟨10.1007/s12104-020-09940-z⟩. ⟨hal-02537946⟩
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