{
  "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.",
  "abstract_shown": true,
  "affiliations": [
    "Instituto de Química Física Blas Cabrera (IQF), CSIC, Madrid, Spain.",
    "Centro de Biología Molecular Severo Ochoa (CBM), CSIC-UAM, Madrid, Spain.",
    "Instituto de Química Física Blas Cabrera (IQF), CSIC, Madrid, Spain. mangeles.jimenez@csic.es."
  ],
  "article_type": "research article",
  "arxiv": null,
  "author_total": 5,
  "authors": [
    {
      "affs": [
        0
      ],
      "name": "Almudena Hornero-Romera"
    },
    {
      "affs": [
        0
      ],
      "name": "Miguel Á Treviño"
    },
    {
      "affs": [
        0
      ],
      "name": "David Pantoja-Uceda"
    },
    {
      "affs": [
        1
      ],
      "name": "Jaime Millán"
    },
    {
      "affs": [
        2
      ],
      "name": "M Ángeles Jiménez",
      "orcid": "0000-0001-6835-5850"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/1d9byk8kgvb2v.bib",
  "cited_by": 0,
  "doi": "10.1007/s12104-026-10281-6",
  "fulltext_url": "https://europepmc.org/articles/PMC13719848",
  "id": "1d9byk8kgvb2v",
  "issns": [
    "1874-2718",
    "1874-270X"
  ],
  "landing_url": "https://europepmc.org/article/MED/42955470",
  "language": "eng",
  "licence": "CC-BY",
  "licence_label": "CC BY",
  "licence_source": "article",
  "licence_url": "https://creativecommons.org/licenses/by/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "heading",
      "Article"
    ],
    [
      "openalex",
      "1312|Protein Structure and Dynamics"
    ]
  ],
  "openalex": "W7224238215",
  "pdf_url": "https://europepmc.org/articles/PMC13719848?pdf=render",
  "pmcid": "PMC13719848",
  "pmid": "42955470",
  "published": "2026-10-29",
  "publisher": null,
  "ris": "https://research.draconitic.com/paper/1d9byk8kgvb2v.ris",
  "sources": [
    {
      "first_seen": "2026-11-01T00:20:36Z",
      "native_id": "MED:42955470",
      "source": "europepmc",
      "url": "https://europepmc.org/article/MED/42955470"
    },
    {
      "first_seen": "2026-11-02T12:23:44Z",
      "native_id": "PMC13719848",
      "source": "pmc",
      "url": "https://doi.org/10.1007/s12104-026-10281-6"
    }
  ],
  "subjects": [
    {
      "field": "biochemistry",
      "origin": "openalex:1312|Protein Structure and Dynamics",
      "subfield": "molecular-biology"
    }
  ],
  "title": "¹H, ¹³C, and ¹⁵N backbone resonance assignment of the N-terminal 280 amino acids of human NHERF1 protein.",
  "title_text": "¹H, ¹³C, and ¹⁵N backbone resonance assignment of the N-terminal 280 amino acids of human NHERF1 protein.",
  "type": "peer-reviewed",
  "updated_at": "2026-11-03T12:20:50Z",
  "url": "https://research.draconitic.com/paper/1d9byk8kgvb2v",
  "venue": "Biomolecular NMR assignments",
  "versions": []
}