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Tytuł pozycji:

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

Tytuł:
N chemical shift assignment of human PACSIN1/syndapin I SH3 domain in solution.
Autorzy:
Boll, Emmanuelle
Cantrelle, Francois-Xavier
Landrieu, Isabelle
Hirel, Matthieu
Sinnaeve, Davy
Levy, Géraldine
Źródło:
Biomolecular NMR Assignments; Oct2020, Vol. 14 Issue 2, p175-178, 4p
Czasopismo naukowe
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. [ABSTRACT FROM AUTHOR]
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