Prediction of binding motifs in hepatitis C virus NS5A and human proteins.
From the extensive analysis, we identified three highly conserved sequence segments in HCV NS5A proteins and one binding motif in human proteins. The binding motif of human proteins often forms a full helix or an extended strand-loop structure, and is in good agreement with the experimental findings of previous studies.
School of Computer Science and Engineering, Inha University, Korea. khan@inha.ac.kr.
Guang-Zheng
GZ
Zhang
Kyungsook
K
Han
D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D019295:Computational Biology / Q000379:methods*; D030562:Databases, Protein; D016174:Hepacivirus / Q000737:chemistry*; D006801:Humans; D008969:Molecular Sequence Data; D011485:Protein Binding; D011487:Protein Conformation; D054730:Protein Interaction Domains and Motifs; D025941:Protein Interaction Mapping; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*; D016415:Sequence Alignment; D017361:Viral Nonstructural Proteins / Q000737:chemistry* / Q000378:metabolism*; D012324:RNA-Dependent RNA Polymerase
D011506:Proteins; D017361:Viral Nonstructural Proteins; C087036:NS-5 protein, hepatitis C virus; D012324:RNA-Dependent RNA Polymerase