Literature DB >> 34739631

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

Jeffrey F Ellena1, Tuo-Xian Tang2,3, Narasimhamurthy Shanaiah4, Daniel G S Capelluto5.   

Abstract

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.
© 2021. The Author(s), under exclusive licence to Springer Nature B.V.

Entities:  

Keywords:  Endosome; FYVE domain; PH domain; Phafin2; Phosphoinositide

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Substances:

Year:  2021        PMID: 34739631      PMCID: PMC9068824          DOI: 10.1007/s12104-021-10054-3

Source DB:  PubMed          Journal:  Biomol NMR Assign        ISSN: 1874-270X            Impact factor:   0.731


  1 in total

1.  Computational Analysis of the Binding Specificities of PH Domains.

Authors:  Zhi Jiang; Zhongjie Liang; Bairong Shen; Guang Hu
Journal:  Biomed Res Int       Date:  2015-12-31       Impact factor: 3.411

  1 in total

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