{
  "abstract": "Complementarity Determining Regions (CDRs) in antibodies, and in particular the CDR-H3 loop, often display conformational plasticity that is essential for their function. Due to this flexibility, the structural investigation of antibody-antigen binding cannot exclusively rely on experimental techniques that only provide snapshots of unbound and bound states, such as X-ray crystallography. Moreover, X-ray structures can be biased due to experimental conditions and crystal packing. In this context, computational techniques, and especially conformational sampling methods, are an essential complement to experiments. This work illustrates the interest of such a coupling of methods on the structural investigation of an anti-FGFR4 (Fibroblast growth factor receptor 4) antibody. X-ray crystallography experiments revealed a very significant conformational change of the CDR-H3 loop between unbound and bound states. Structural bioinformatics methods were then applied to provide a more global picture of the conformational space of this loop, and to confirm that the observed",
  "abstract_shown": true,
  "affiliations": [],
  "article_type": null,
  "arxiv": null,
  "author_total": 10,
  "authors": [
    {
      "name": "Amélie Barozet"
    },
    {
      "name": "Magali Mathieu"
    },
    {
      "name": "David Papin"
    },
    {
      "name": "Béatrice Cameron"
    },
    {
      "name": "Tarik Dabdoubi"
    },
    {
      "name": "Anne Séverac"
    },
    {
      "name": "Paul Ferrari"
    },
    {
      "name": "Thierry Siméon"
    },
    {
      "name": "Marc Bianciotto"
    },
    {
      "name": "Juan Cortés"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/8ekge6dtzt8rk.bib",
  "cited_by": 0,
  "doi": "10.1016/j.jsb.2026.108368",
  "fulltext_url": null,
  "id": "8ekge6dtzt8rk",
  "issns": [
    "1047-8477",
    "1095-8657"
  ],
  "landing_url": "https://laas.hal.science/hal-05752121v1",
  "language": "en",
  "licence": "CC-BY-4.0",
  "licence_label": "CC BY 4.0",
  "licence_source": "article",
  "licence_url": "https://creativecommons.org/licenses/by/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "hal",
      "0.info"
    ],
    [
      "hal",
      "0.sdv"
    ],
    [
      "hal",
      "1.info.info-ai"
    ],
    [
      "hal",
      "1.info.info-bi"
    ],
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      "hal",
      "1.sdv.bbm"
    ],
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      "hal",
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    ],
    [
      "openalex",
      "1312|Protein Structure and Dynamics"
    ]
  ],
  "openalex": "W7212391652",
  "pdf_url": "https://laas.hal.science/hal-05752121/document",
  "pmcid": null,
  "pmid": null,
  "published": "2026-09-12",
  "publisher": "Elsevier",
  "ris": "https://research.draconitic.com/paper/8ekge6dtzt8rk.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:17:35Z",
      "native_id": "hal-05752121",
      "source": "hal",
      "url": "https://laas.hal.science/hal-05752121v1"
    }
  ],
  "subjects": [
    {
      "field": "biochemistry",
      "origin": "hal:2.sdv.bbm.bs",
      "subfield": "structural-biology"
    },
    {
      "field": "biology",
      "origin": "hal:0.sdv",
      "subfield": "general"
    }
  ],
  "title": "Antibody CDR-H3 loop flexibility: Insights from X-ray crystallography, structural bioinformatics, and the limits of current deep learning methods",
  "title_text": "Antibody CDR-H3 loop flexibility: Insights from X-ray crystallography, structural bioinformatics, and the limits of current deep learning methods",
  "type": "peer-reviewed",
  "updated_at": "2026-10-30T12:17:35Z",
  "url": "https://research.draconitic.com/paper/8ekge6dtzt8rk",
  "venue": "Journal of Structural Biology",
  "versions": []
}