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作者:

Wang Pan-Wen (Wang Pan-Wen.) | Gong Xin-Qi (Gong Xin-Qi.) | Li Chun-Hua (Li Chun-Hua.) (学者:李春华) | Chen Wei-Zu (Chen Wei-Zu.) | Wang Cun-Xin (Wang Cun-Xin.)

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Scopus SCIE PKU CSCD

摘要:

Binding site prediction for protein-protein complexes is a challenging problem in the area of computational molecular biology. Using a set of double-chain complexes in Benchmark 3.0, we calculated the solvent accessible surface areas and inter-residue contact areas for each monomer and propose a division method of protein surface patches. We found that the products of the solvent accessible surface areas and internal contact areas of patches, the PSAIA values, could provide protein binding site information. In a dataset of 78 complexes, either receptors or ligands of 74 complexes had interface patches with the first or second greatest PSAIA values among all surface patches. A good docking result was achieved when the binding site information obtained with this method was applied in Target 39 of the CAPRI experiment. This patch-based protein binding site prediction method differs from traditional methods, which are based on single residue and consider only surface residues. This provides a new method for binding site prediction in protein-protein interactions.

关键词:

Solvent accessible surface area Patch division Interior contact area Protein binding site prediction

作者机构:

  • [ 1 ] [Wang Pan-Wen]Beijing Univ Technol, Coll Life Sci & Bioengn, Beijing 100124, Peoples R China
  • [ 2 ] [Li Chun-Hua]Beijing Univ Technol, Coll Life Sci & Bioengn, Beijing 100124, Peoples R China
  • [ 3 ] [Chen Wei-Zu]Beijing Univ Technol, Coll Life Sci & Bioengn, Beijing 100124, Peoples R China
  • [ 4 ] [Wang Cun-Xin]Beijing Univ Technol, Coll Life Sci & Bioengn, Beijing 100124, Peoples R China
  • [ 5 ] [Gong Xin-Qi]Tsinghua Univ, Sch Life Sci, Beijing 100084, Peoples R China

通讯作者信息:

  • 李春华

    [Li Chun-Hua]Beijing Univ Technol, Coll Life Sci & Bioengn, Beijing 100124, Peoples R China

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来源 :

ACTA PHYSICO-CHIMICA SINICA

ISSN: 1000-6818

年份: 2012

期: 11

卷: 28

页码: 2729-2734

1 0 . 9 0 0

JCR@2022

ESI学科: CHEMISTRY;

JCR分区:4

中科院分区:4

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SCOPUS被引频次: 1

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