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LABind: identifying protein binding ligand-aware sites via learning interactions between ligand and protein

Author

Listed:
  • Zhijun Zhang

    (Soochow University)

  • Lijun Quan

    (Soochow University
    Collaborative Innovation Center of Novel Software Technology and Industrialization
    Soochow University)

  • Junkai Wang

    (Soochow University)

  • Liangchen Peng

    (Soochow University)

  • Qiufeng Chen

    (Soochow University)

  • Bei Zhang

    (Soochow University)

  • Lexin Cao

    (Soochow University)

  • Yelu Jiang

    (Soochow University)

  • Geng Li

    (Soochow University)

  • Liangpeng Nie

    (Soochow University)

  • Tingfang Wu

    (Soochow University
    Collaborative Innovation Center of Novel Software Technology and Industrialization
    Soochow University)

  • Qiang Lyu

    (Soochow University
    Collaborative Innovation Center of Novel Software Technology and Industrialization
    Soochow University)

Abstract

Protein-ligand interactions are crucial for understanding various biological processes and drug discovery and design. However, experimental methods are costly; single-ligand-oriented methods are tailored to specific ligands; multi-ligand-oriented methods are constrained by the lack of ligand encoding. In this study, we propose a structure-based method called LABind, designed to predict binding sites for small molecules and ions in a ligand-aware manner. LABind utilizes a graph transformer to capture binding patterns within the local spatial context of proteins, and incorporates a cross-attention mechanism to learn the distinct binding characteristics between proteins and ligands. Experimental results on three benchmark datasets demonstrate both the effectiveness of LABind and its ability to generalize to unseen ligands. Further analysis validates that LABind can effectively integrate ligand information to predict binding sites. Additionally, the application of LABind is extended to binding site center localization, sequence-based methods, and molecular docking tasks.

Suggested Citation

  • Zhijun Zhang & Lijun Quan & Junkai Wang & Liangchen Peng & Qiufeng Chen & Bei Zhang & Lexin Cao & Yelu Jiang & Geng Li & Liangpeng Nie & Tingfang Wu & Qiang Lyu, 2025. "LABind: identifying protein binding ligand-aware sites via learning interactions between ligand and protein," Nature Communications, Nature, vol. 16(1), pages 1-14, December.
  • Handle: RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-62899-0
    DOI: 10.1038/s41467-025-62899-0
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    1. Takaya Saito & Marc Rehmsmeier, 2015. "The Precision-Recall Plot Is More Informative than the ROC Plot When Evaluating Binary Classifiers on Imbalanced Datasets," PLOS ONE, Public Library of Science, vol. 10(3), pages 1-21, March.
    2. Ryunosuke Hayashi & Shohei Tashiro & Masahiro Asakura & Shinya Mitsui & Mitsuhiko Shionoya, 2023. "Effector-dependent structural transformation of a crystalline framework with allosteric effects on molecular recognition ability," Nature Communications, Nature, vol. 14(1), pages 1-9, December.
    3. Kouji Hirota & Tomoichiro Miyoshi & Kazuto Kugou & Charles S. Hoffman & Takehiko Shibata & Kunihiro Ohta, 2008. "Stepwise chromatin remodelling by a cascade of transcription initiation of non-coding RNAs," Nature, Nature, vol. 456(7218), pages 130-134, November.
    4. James A. Wells & Christopher L. McClendon, 2007. "Reaching for high-hanging fruit in drug discovery at protein–protein interfaces," Nature, Nature, vol. 450(7172), pages 1001-1009, December.
    5. John Jumper & Richard Evans & Alexander Pritzel & Tim Green & Michael Figurnov & Olaf Ronneberger & Kathryn Tunyasuvunakool & Russ Bates & Augustin Žídek & Anna Potapenko & Alex Bridgland & Clemens Me, 2021. "Highly accurate protein structure prediction with AlphaFold," Nature, Nature, vol. 596(7873), pages 583-589, August.
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