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

被引：0

作者：

Jeffrey F. Ellena

Tuo-Xian Tang

Narasimhamurthy Shanaiah

Daniel G. S. Capelluto

机构：

[1] University of Virginia,Biomolecular Magnetic Resonance Facility

[2] Virginia Tech,Protein Signaling Domains Laboratory, Department of Biological Sciences, Fralin Life Sciences Institute and Center for Soft Matter and Biological Physics

[3] Virginia Tech,Department of Chemistry

[4] University of Pennsylvania,Department of Biology

来源：

Biomolecular NMR Assignments | 2022年 / 16卷

关键词：

Phafin2; PH domain; FYVE domain; Endosome; Phosphoinositide;

D O I：

暂无

中图分类号：

学科分类号：

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 1H, 15N, and 13C backbone resonance assignments.

引用

页码：27 / 30

页数：3

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