¹H, ¹³C, and ¹⁵N backbone resonance assignment of the N-terminal 280 amino acids of human NHERF1 protein.
- 1Instituto de Química Física Blas Cabrera (IQF), CSIC, Madrid, Spain.
- 2Centro de Biología Molecular Severo Ochoa (CBM), CSIC-UAM, Madrid, Spain.
- 3Instituto de Química Física Blas Cabrera (IQF), CSIC, Madrid, Spain. [email protected].
Abstract
NHERF1 (Na+/H+ exchanger regulatory factor-1) is a membrane-associated scaffold protein that links membrane receptors and channels to the actin cytoskeleton. It plays key roles in protein trafficking, signaling, and liver physiology. NHERF1 is a 358-residue long multidomain protein consisting of two PDZ domains, followed by a largely disordered region and a C-terminal ezrin-binding (EB) domain. In the liver, NHERF1 promotes the assembly of complexes containing ERM (ezrin-radixin-moesin) proteins, ICAM-1 (type I transmembrane protein intercellular adhesion molecule), and F-actin. Recent pull-down experiments have suggested that both PDZ1 and PDZ2 domains contribute to ICAM-1 binding. Characterization of this interaction by NMR chemical shift mapping requires a construct containing both PDZ domains. Although NMR studies have previously been reported for the individual PDZ1 and PDZ2 domains, as well as for the full-length NHERF1, no assignments were available for a construct containing only the PDZ domains. Full-length NHERF1 is not adequate for investigating PDZ-mediated interactions because its C-terminal EB domain interacts with PDZ2, causing resonance line broadening. In addition, the full-length 358-residue protein is expected to exhibit greater spectral overlap than a shorter construct. Here, we report the ¹H, ¹⁵N, and ¹³C backbone resonance assignments of a N-terminal 280 residue long NHERF1 construct encompassing both the PDZ1 and PDZ2 domains, thereby facilitating future studies of its interactions with ICAM-1 and other binding partners.
Related
- Backbone and side-chain NMR resonance assignments of Ciona intestinalis\documentclass[12pt]{minimal} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{upgreek} \setlength{\oddsidemargin}{-69pt} \begin{document}β γ\end{document}-crystallin
- GeoDSSOP: Geometry-aware prediction of protein backbone order parameters from sequence and structure
- Who contributes to whom: following the evidence behind protein language-model predictions of backbone variability
- An evolutionary strategy for highly efficient secretion of multidomain Staphylococcal protein A: N- to C-terminal stability gradient
- Terminal hydroxylation of eIF5A hypusination influences mitochondrial protein expression and cellular metabolism in fission yeast
BibTeX
@article{horneroromera2026¹³c,
title = {{¹H, ¹³C, and ¹⁵N backbone resonance assignment of the N-terminal 280 amino acids of human NHERF1 protein.}},
author = {Almudena Hornero-Romera and Miguel Á Treviño and David Pantoja-Uceda and Jaime Millán and M Ángeles Jiménez},
journal = {Biomolecular NMR assignments},
year = {2026},
month = oct,
doi = {10.1007/s12104-026-10281-6},
url = {https://europepmc.org/article/MED/42955470},
note = {CC BY},
}
RIS
TY - JOUR
TI - ¹H, ¹³C, and ¹⁵N backbone resonance assignment of the N-terminal 280 amino acids of human NHERF1 protein.
AU - Almudena Hornero-Romera
AU - Miguel Á Treviño
AU - David Pantoja-Uceda
AU - Jaime Millán
AU - M Ángeles Jiménez
PY - 2026
DA - 2026/10/29
JO - Biomolecular NMR assignments
DO - 10.1007/s12104-026-10281-6
UR - https://europepmc.org/article/MED/42955470
AB - NHERF1 (Na+/H+ exchanger regulatory factor-1) is a membrane-associated scaffold protein that links membrane receptors and channels to the actin cytoskeleton. It plays key roles in protein trafficking, signaling, and liver physiology. NHERF1 is a 358-residue long multidomain protein consisting of two PDZ domains, followed by a largely disordered region and a C-terminal ezrin-binding (EB) domain. In the liver, NHERF1 promotes the assembly of complexes containing ERM (ezrin-radixin-moesin) proteins, ICAM-1 (type I transmembrane protein intercellular adhesion molecule), and F-actin. Recent pull-down experiments have suggested that both PDZ1 and PDZ2 domains contribute to ICAM-1 binding. Characterization of this interaction by NMR chemical shift mapping requires a construct containing both PDZ domains. Although NMR studies have previously been reported for the individual PDZ1 and PDZ2 domains, as well as for the full-length NHERF1, no assignments were available for a construct containing only the PDZ domains. Full-length NHERF1 is not adequate for investigating PDZ-mediated interactions because its C-terminal EB domain interacts with PDZ2, causing resonance line broadening. In addition, the full-length 358-residue protein is expected to exhibit greater spectral overlap than a shorter construct. Here, we report the ¹H, ¹⁵N, and ¹³C backbone resonance assignments of a N-terminal 280 residue long NHERF1 construct encompassing both the PDZ1 and PDZ2 domains, thereby facilitating future studies of its interactions with ICAM-1 and other binding partners.
SN - 1874-2718
SN - 1874-270X
ER -