{
  "abstract": "F-box proteins, the substrate-recognition modules of the SCF (Skp1-Cul1-F-box) ubiquitin ligase complex, play a central role in targeted protein degradation by enabling the selective recruitment of diverse substrates. F-box proteins share a common architecture with a conserved anchor domain linked to the substrate-binding domain. Despite extensive structural characterization of F-box proteins, their potential conformational dynamics remain poorly understood. Here, we employ an integrative modeling approach combining cryo-EM structures, cross-linking mass spectrometry (XL-MS), and deep learning-based conformational ensemble prediction to profile the accessible conformations of F-box proteins. Our analyses reveal a significant inter-domain flexibility in FBXL2 and FBXL17 that enables sampling of a broad range of conformations within assembled SCF and CSN-SCF complexes. By contrast, other F-box proteins, including FBXL1 and FBXO22, exhibit intrinsic flexibility but are restricted to a considerably narrower conformational landscape. Together, our work highlights inter-domain plasticity as a tunable architectural feature of F-box proteins, which may shape their functional versatility within SCF complexes.",
  "abstract_shown": true,
  "affiliations": [
    "The Hebrew University of Jerusalem"
  ],
  "article_type": "New results",
  "arxiv": null,
  "author_total": 9,
  "authors": [
    {
      "name": "B. Shor"
    },
    {
      "name": "F. Jiao"
    },
    {
      "name": "H. Shi"
    },
    {
      "name": "H. Mao"
    },
    {
      "name": "C. Yu"
    },
    {
      "name": "M. Braitbard"
    },
    {
      "name": "L. Huang"
    },
    {
      "name": "N. Zheng"
    },
    {
      "affs": [
        0
      ],
      "name": "D. Schneidman-Duhovny"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/4tcza4ng5sfdp.bib",
  "cited_by": 0,
  "doi": "10.64898/2026.11.07.764542",
  "fulltext_url": "https://www.biorxiv.org/content/10.64898/2026.11.07.764542v1.full",
  "id": "4tcza4ng5sfdp",
  "issns": [],
  "landing_url": "https://www.biorxiv.org/content/10.64898/2026.11.07.764542v1",
  "language": null,
  "licence": "CC-BY",
  "licence_label": "CC BY",
  "licence_source": "article",
  "licence_url": "https://creativecommons.org/licenses/by/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "biorxiv",
      "molecular biology"
    ]
  ],
  "openalex": null,
  "pdf_url": "https://www.biorxiv.org/content/10.64898/2026.11.07.764542v1.full.pdf",
  "pmcid": null,
  "pmid": null,
  "published": "2026-11-07",
  "publisher": null,
  "ris": "https://research.draconitic.com/paper/4tcza4ng5sfdp.ris",
  "sources": [
    {
      "first_seen": "2026-11-10T00:28:02Z",
      "native_id": "10.64898/2026.11.07.764542",
      "source": "biorxiv",
      "url": "https://www.biorxiv.org/content/10.64898/2026.11.07.764542v1"
    }
  ],
  "subjects": [
    {
      "field": "biochemistry",
      "origin": "biorxiv:molecular biology",
      "subfield": "molecular-biology"
    }
  ],
  "title": "Inter-domain flexibility in F-Box proteins revealed by integrative modeling",
  "title_text": "Inter-domain flexibility in F-Box proteins revealed by integrative modeling",
  "type": "preprint",
  "updated_at": "2026-11-10T00:28:02Z",
  "url": "https://research.draconitic.com/paper/4tcza4ng5sfdp",
  "venue": "bioRxiv",
  "versions": []
}