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, ¹³C_α and ¹³C_β, 28% of ¹³C_γδε, 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.

中文翻译：

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溶液中人 PACSIN1/syndapin I SH3 结构域的 1H、13C 和 15N 化学位移分配。

人类神经元特异性 PACSIN1 在突触囊泡循环和内吞作用以及微管动力学重组以维持轴突可塑性中起着关键作用。PACSIN1 在其 N 端包含一个高度保守的 C 端 SH3 结构域和一个 F-bar 结构域。由于其卓越的相互作用网络，PACSIN1 在关键神经元功能中发挥着核心作用。在这里，我们基于 2D [ ¹ H, ¹⁵ N] HSQC 或 HMQC 和 3D BEST-HNCO、-HNCACB、-HN(CO)CACB、-HN(CA )CO，和标准 (H)CC(CO)NH、HN(CA)NNH、HN(COCA)NH、HBHANNH、HNHA、HBHA(CO)NH、H(CC)(CO)NH、HCCH-TOCSY，即覆盖所有¹³ CO、¹³ C _α和¹³ C 的96%_β、28% 的¹³ C _γδε和 95% 的¹ HN 和¹⁵ N 化学位移。基于具有已知相关结构的序列同源性和基于化学位移的二级结构预测的建模，确定了由柔性环连接的五个 β 链的存在。总之，这些结果为研究和开发新的治疗策略开辟了新的途径。