Phafin2 pleckstrin 同源结构域的骨架 H、N 和 C 共振峰分配。
Backbone H, N, and C resonance assignments of the Phafin2 pleckstrin homology domain.
机构信息
Biomolecular Magnetic Resonance Facility, University of Virginia, Charlottesville, VA, 22904, USA.
Protein Signaling Domains Laboratory, Department of Biological Sciences, Fralin Life Sciences Institute and Center for Soft Matter and Biological Physics, Virginia Tech, Blacksburg, VA, 24061, USA.
出版信息
Biomol NMR Assign. 2022 Apr;16(1):27-30. doi: 10.1007/s12104-021-10054-3. Epub 2021 Nov 5.
Phafin2 is a peripheral protein that triggers cellular signaling from endosomal and lysosomal compartments. The specific subcellular localization of Phafin2 is mediated by the presence of a tandem of phosphatidylinositol 3-phosphate (PtdIns3P)-binding domains, the pleckstrin homology (PH) and the Fab-1, YOTB, Vac1, and EEA1 (FYVE) domains. The requirement for both domains for binding to PtdIns3P still remains unclear. To understand the molecular interactions of the Phafin2 PH domain in detail, we report its nearly complete H, N, and C backbone resonance assignments.
Phafin2 是一种外周蛋白，可从内体和溶酶体隔室触发细胞信号转导。Phafin2 的特定亚细胞定位是由串联的两个磷脂酰肌醇 3-磷酸（PtdIns3P）结合结构域、pleckstrin 同源（PH）和 Fab-1、YOTB、Vac1 和 EEA1（FYVE）结构域介导的。对于结合 PtdIns3P 来说，这两个结构域都是必需的，但它们的结合机制仍不清楚。为了详细了解 Phafin2 PH 结构域的分子相互作用，我们报道了其几乎完整的 H、N 和 C 骨架共振归属。
Zotero 插件