Backbone H-1, N-15, and C-13 resonance assignments of the Phafin2 pleckstrin homology domain

被引：2
|
作者：
Ellena, Jeffrey F. [1 ]
Tang, Tuo-Xian [2 ,3 ,5 ]
Shanaiah, Narasimhamurthy [4 ]
Capelluto, Daniel G. S. [2 ,3 ]
机构：
[1] Univ Virginia, Biomol Magnet Resonance Facil, Charlottesville, VA 22904 USA
[2] Virginia Tech, Prot Signaling Domains Lab, Dept Biol Sci, Fralin Life Sci Inst, Blacksburg, VA 24061 USA
[3] Virginia Tech, Ctr Soft Matter & Biol Phys, Blacksburg, VA 24061 USA
[4] Virginia Tech, Dept Chem, Blacksburg, VA 24061 USA
[5] Univ Penn, Dept Biol, Philadelphia, PA 19104 USA
来源：
BIOMOLECULAR NMR ASSIGNMENTS | 2022年 / 16卷 / 01期
关键词：
Phafin2; PH domain; FYVE domain; Endosome; Phosphoinositide; PROTEIN; PH;
D O I：
10.1007/s12104-021-10054-3
中图分类号：
Q6 [生物物理学];
学科分类号：
071011 ;
摘要：
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-1, N-15, and C-13 backbone resonance assignments.
引用
收藏
页码：27 / 30
页数：4
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