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
相关论文
共 50 条
  • [21] H-1, C-13, AND N-15 RESONANCE ASSIGNMENTS FOR A FERROCYTOCHROME-C553 HEME BY MULTINUCLEAR NMR-SPECTROSCOPY
    ZEHFUS, MH
    REILY, MD
    ULRICH, EL
    WESTLER, WM
    MARKLEY, JL
    ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1990, 276 (02) : 369 - 373
  • [22] The H-1, N-15 and C-13 resonance assignments of the low-complexity domain from the oncogenic fusion protein EWS-FLI1
    Johnson, Courtney N.
    Xu, Xiaoping
    Holloway, Stephen P.
    Libich, David S.
    BIOMOLECULAR NMR ASSIGNMENTS, 2022, 16 (01) : 67 - 73
  • [23] BACKBONE H-1, C-13, AND N-15 ASSIGNMENTS AND SECONDARY STRUCTURE OF BOVINE LOW-MOLECULAR-WEIGHT PHOSPHOTYROSYL PROTEIN PHOSPHATASE
    ZHOU, MM
    LOGAN, TM
    THERIAULT, Y
    VANETTEN, RL
    FESIK, SW
    BIOCHEMISTRY, 1994, 33 (17) : 5221 - 5229
  • [24] Backbone and sidechain H-1, N-15 and C-13 resonance assignments of the free and RNA-bound tandem zinc finger domain of the tristetraprolin family member from Selaginella moellendorffii
    Hicks, Stephanie N.
    Venters, Ronald A.
    Blackshear, Perry J.
    BIOMOLECULAR NMR ASSIGNMENTS, 2022, 16 (01) : 153 - 158
  • [25] H-1, N-15, C-13 AND (CO)-C-13 RESONANCE ASSIGNMENTS AND SECONDARY STRUCTURE OF VILLIN-14T, A DOMAIN CONSERVED AMONG ACTIN-SEVERING PROTEINS
    MARKUS, MA
    NAKAYAMA, T
    MATSUDAIRA, P
    WAGNER, G
    JOURNAL OF BIOMOLECULAR NMR, 1994, 4 (04) : 553 - 574
  • [26] Full assignments of the H-1, C-13 and N-15 NMR spectra of some protonated and unprotonated nitrobenzimidazoles
    Wiench, JW
    Bocian, W
    Stefaniak, L
    Webb, GA
    BULLETIN OF THE POLISH ACADEMY OF SCIENCES-CHEMISTRY, 1995, 43 (04): : 287 - 293
  • [27] H-1, C-13, N-15 RESONANCE ASSIGNMENTS AND SECONDARY STRUCTURE OF S100-BETA BY NMR-SPECTROSCOPY
    AMBURGEY, JC
    ABILDGAARD, F
    STARICH, MR
    SHAH, S
    HILT, DC
    WEBER, DJ
    FASEB JOURNAL, 1995, 9 (06): : A1430 - A1430
  • [28] H-1, N-15 and C-13 resonance assignments and secondary structure determination of the RNA-binding domain of E-coli rho protein
    Briercheck, DM
    Allison, TJ
    Richardson, JP
    Ellena, JF
    Wood, TC
    Rule, GS
    JOURNAL OF BIOMOLECULAR NMR, 1996, 8 (04) : 429 - 444
  • [29] Complete H-1, C-13, and N-15 NMR resonance assignments and secondary structure of human glutaredoxin in the fully reduced form
    Sun, CH
    Holmgren, A
    Bushweller, JH
    PROTEIN SCIENCE, 1997, 6 (02) : 383 - 390
  • [30] H-1, C-13, and N-15 assignments for the Ca2+-bound form of oncomodulin, a beta-parvalbumin
    Henzl, MT
    Likos, JJ
    Hutton, WC
    PROTEIN AND PEPTIDE LETTERS, 1996, 3 (01): : 59 - 66
12345