We present FORTE, a profile-profile comparison tool for protein fold recognition. Users can submit a protein sequence to explore the possibilities of structural similarity existing in known structures. Results are reported via email in the form of pairwise alignments.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1093/bioinformatics/btg474 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Structural Modeling and Ligand-Binding Prediction for Analysis of Structure-Unknown and Function-Unknown Proteins Using FORTE Alignment and PoSSuM Pocket Search.
Methods Mol Biol
March 2021
Artificial Intelligence Research Center, National Institute of Advanced Industrial Science and Technology (AIST), Tokyo, Japan.
Structural data of biomolecules, such as those of proteins and nucleic acids, provide much information for estimation of their functions. For structure-unknown proteins, structure information is obtainable by modeling their structures based on sequence similarity of proteins. Moreover, information related to ligands or ligand-binding sites is necessary to elucidate protein functions because the binding of ligands can engender not only the activation and inactivation of the proteins but also the modification of protein functions.
View Article and Find Full Text PDFTemplate-based quaternary structure prediction of proteins using enhanced profile-profile alignments.
Proteins
March 2018
Artificial Intelligence Research Center (AIRC), National Institute of Advanced Industrial Science and Technology (AIST), 2-4-7 Aomi, Koto-ku, Tokyo, 135-0064, Japan.
Proteins often exist as their multimeric forms when they function as so-called biological assemblies consisting of the specific number and arrangement of protein subunits. Consequently, elucidating biological assemblies is necessary to improve understanding of protein function. Template-Based Modeling (TBM), based on known protein structures, has been used widely for protein structure prediction.
View Article and Find Full Text PDFSAHG, a comprehensive database of predicted structures of all human proteins.
Nucleic Acids Res
January 2011
Computational Biology Research Center, National Institute of Advanced Industrial Science and Technology, Tokyo 135-0064, Japan.
Most proteins from higher organisms are known to be multi-domain proteins and contain substantial numbers of intrinsically disordered (ID) regions. To analyse such protein sequences, those from human for instance, we developed a special protein-structure-prediction pipeline and accumulated the products in the Structure Atlas of Human Genome (SAHG) database at http://bird.cbrc.
View Article and Find Full Text PDFFORTE: a profile-profile comparison tool for protein fold recognition.
Bioinformatics
March 2004
Computational Biology Research Center, The National Institute of Advanced Industrial Science and Technology, Aomi Frontier Building 2-43 Aomi, 17F, Koto-ku, Tokyo 135-0064, Japan.
We present FORTE, a profile-profile comparison tool for protein fold recognition. Users can submit a protein sequence to explore the possibilities of structural similarity existing in known structures. Results are reported via email in the form of pairwise alignments.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!