Conservation of hot regions in protein-protein interaction in evolution

被引:13
作者
Hu, Jing [1 ,2 ]
Li, Jiarui [3 ]
Chen, Nansheng [3 ]
Zhang, Xiaolong [1 ,2 ]
机构
[1] Wuhan Univ Sci & Technol, Sch Comp Sci & Technol, Wuhan, Peoples R China
[2] Hubei Prov Key Lab Intelligent Informat Proc & Re, Wuhan, Peoples R China
[3] Simon Fraser Univ, Dept Mol Biol & Biochem, Burnaby, BC, Canada
基金
中国国家自然科学基金;
关键词
Hot region; Protein-protein interaction; Conservation; Evolution; PREDICTION; ORGANIZATION; DATABASE; BINDING; SITES;
D O I
10.1016/j.ymeth.2016.06.020
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
The hot regions of protein-protein interactions refer to the active area which formed by those most important residues to protein combination process. With the research development on protein interactions, lots of predicted hot regions can be discovered efficiently by intelligent computing methods, while performing biology experiments to verify each every prediction is hardly to be done due to the time-cost and the complexity of the experiment. This study based on the research of hot spot residue conservations, the proposed method is used to verify authenticity of predicted hot regions that using machine learning algorithm combined with protein's biological features and sequence conservation, though multiple sequence alignment, module substitute matrix and sequence similarity to create conservation scoring algorithm, and then using threshold module to verify the conservation tendency of hot regions in evolution. This research work gives an effective method to verify predicted hot regions in protein-protein interactions, which also provides a useful way to deeply investigate the functional activities of protein hot regions. (C) 2016 Published by Elsevier Inc.
引用
收藏
页码:73 / 80
页数:8
相关论文
共 22 条
  • [1] Automated structure-based prediction of functional sites in proteins: Applications to assessing the validity of inheriting protein function from homology in genome annotation and to protein docking
    Aloy, P
    Querol, E
    Aviles, FX
    Sternberg, MJE
    [J]. JOURNAL OF MOLECULAR BIOLOGY, 2001, 311 (02) : 395 - 408
  • [2] The Protein Data Bank
    Berman, HM
    Westbrook, J
    Feng, Z
    Gilliland, G
    Bhat, TN
    Weissig, H
    Shindyalov, IN
    Bourne, PE
    [J]. NUCLEIC ACIDS RESEARCH, 2000, 28 (01) : 235 - 242
  • [3] Anatomy of hot spots in protein interfaces
    Bogan, AA
    Thorn, KS
    [J]. JOURNAL OF MOLECULAR BIOLOGY, 1998, 280 (01) : 1 - 9
  • [4] Are protein-protein interfaces more conserved in sequence than the rest of the protein surface?
    Caffrey, DR
    Somaroo, S
    Hughes, JD
    Mintseris, J
    Huang, ES
    [J]. PROTEIN SCIENCE, 2004, 13 (01) : 190 - 202
  • [5] OrthoMCL-DB: querying a comprehensive multi-species collection of ortholog groups
    Chen, Feng
    Mackey, Aaron J.
    Stoeckert, Christian J., Jr.
    Roos, David S.
    [J]. NUCLEIC ACIDS RESEARCH, 2006, 34 : D363 - D368
  • [6] HotRegion: a database of predicted hot spot clusters
    Cukuroglu, Engin
    Gursoy, Attila
    Keskin, Ozlem
    [J]. NUCLEIC ACIDS RESEARCH, 2012, 40 (D1) : D829 - D833
  • [7] Analysis of Hot Region Organization in Hub Proteins
    Cukuroglu, Engin
    Gursoy, Attila
    Keskin, Ozlem
    [J]. ANNALS OF BIOMEDICAL ENGINEERING, 2010, 38 (06) : 2068 - 2078
  • [8] Dongfang Nan, 2013, 2013 IEEE International Conference on Bioinformatics and Biomedicine (BIBM), P17, DOI 10.1109/BIBM.2013.6732712
  • [9] Fischer Steve, 2011, Curr Protoc Bioinformatics, VChapter 6, DOI 10.1002/0471250953.bi0612s35
  • [10] AMINO-ACID SUBSTITUTION MATRICES FROM PROTEIN BLOCKS
    HENIKOFF, S
    HENIKOFF, JG
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1992, 89 (22) : 10915 - 10919