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  1. 研究報告
  2. バイオ情報学(BIO)
  3. 2024
  4. 2024-BIO-78

SpatialPPI: Three-dimensional space protein-protein interaction prediction with AlphaFold Multimer

https://ipsj.ixsq.nii.ac.jp/records/234840
https://ipsj.ixsq.nii.ac.jp/records/234840
dc6f4914-44a8-4ea6-9087-524161b64e2f
名前 / ファイル ライセンス アクション
IPSJ-BIO24078013.pdf IPSJ-BIO24078013.pdf (7.3 MB)
 2026年6月13日からダウンロード可能です。
Copyright (c) 2024 by the Information Processing Society of Japan
非会員:¥660, IPSJ:学会員:¥330, BIO:会員:¥0, DLIB:会員:¥0
Item type SIG Technical Reports(1)
公開日 2024-06-13
タイトル
タイトル SpatialPPI: Three-dimensional space protein-protein interaction prediction with AlphaFold Multimer
タイトル
言語 en
タイトル SpatialPPI: Three-dimensional space protein-protein interaction prediction with AlphaFold Multimer
言語
言語 eng
キーワード
主題Scheme Other
主題 バイオ情報学1
資源タイプ
資源タイプ識別子 http://purl.org/coar/resource_type/c_18gh
資源タイプ technical report
著者所属
Department of Computer Science, School of Computing, Tokyo Institute of Technology
著者所属
Department of Computer Science, School of Computing, Tokyo Institute of Technology
著者所属(英)
en
Department of Computer Science, School of Computing, Tokyo Institute of Technology
著者所属(英)
en
Department of Computer Science, School of Computing, Tokyo Institute of Technology
著者名 Wenxing, Hu

× Wenxing, Hu

Wenxing, Hu

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Masahito, Ohue

× Masahito, Ohue

Masahito, Ohue

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著者名(英) Wenxing, Hu

× Wenxing, Hu

en Wenxing, Hu

Search repository
Masahito, Ohue

× Masahito, Ohue

en Masahito, Ohue

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論文抄録
内容記述タイプ Other
内容記述 Rapid advancements in protein sequencing technology have resulted in gaps between proteins with identified sequences and those with mapped structures. Although sequence-based predictions offer insights, they can be incomplete due to the absence of structural details. Conversely, structure-based methods face challenges with respect to newly sequenced proteins. The AlphaFold Multimer has remarkable accuracy in predicting the structure of protein complexes. However, it cannot distinguish whether the input protein sequences can interact. Nonetheless, by analyzing the information in the models predicted by the AlphaFold Multimer, we propose a highly accurate method for predicting protein interactions. This study focuses on the use of deep neural networks, specifically to analyze protein complex structures predicted by the AlphaFold Multimer. By transforming atomic coordinates and utilizing sophisticated image-processing techniques, vital 3D structural details were extracted from protein complexes. Recognizing the significance of evaluating residue distances in protein interactions, this study leveraged image recognition approaches by integrating Densely Connected Convolutional Networks (DenseNet) and Deep Residual Network (ResNet) within 3D convolutional networks for protein 3D structure analysis. When benchmarked against leading protein-protein interaction prediction methods, such as SpeedPPI, D-script, DeepTrio, and PEPPI, our proposed method, named SpatialPPI, exhibited notable efficacy, emphasizing the promising role of 3D spatial processing in advancing the realm of structural biology.
論文抄録(英)
内容記述タイプ Other
内容記述 Rapid advancements in protein sequencing technology have resulted in gaps between proteins with identified sequences and those with mapped structures. Although sequence-based predictions offer insights, they can be incomplete due to the absence of structural details. Conversely, structure-based methods face challenges with respect to newly sequenced proteins. The AlphaFold Multimer has remarkable accuracy in predicting the structure of protein complexes. However, it cannot distinguish whether the input protein sequences can interact. Nonetheless, by analyzing the information in the models predicted by the AlphaFold Multimer, we propose a highly accurate method for predicting protein interactions. This study focuses on the use of deep neural networks, specifically to analyze protein complex structures predicted by the AlphaFold Multimer. By transforming atomic coordinates and utilizing sophisticated image-processing techniques, vital 3D structural details were extracted from protein complexes. Recognizing the significance of evaluating residue distances in protein interactions, this study leveraged image recognition approaches by integrating Densely Connected Convolutional Networks (DenseNet) and Deep Residual Network (ResNet) within 3D convolutional networks for protein 3D structure analysis. When benchmarked against leading protein-protein interaction prediction methods, such as SpeedPPI, D-script, DeepTrio, and PEPPI, our proposed method, named SpatialPPI, exhibited notable efficacy, emphasizing the promising role of 3D spatial processing in advancing the realm of structural biology.
書誌レコードID
収録物識別子タイプ NCID
収録物識別子 AA12055912
書誌情報 研究報告バイオ情報学(BIO)

巻 2024-BIO-78, 号 13, p. 1-8, 発行日 2024-06-13
ISSN
収録物識別子タイプ ISSN
収録物識別子 2188-8590
Notice
SIG Technical Reports are nonrefereed and hence may later appear in any journals, conferences, symposia, etc.
出版者
言語 ja
出版者 情報処理学会
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