Yassine Ghouzam1, Guillaume Postic1, Alexandre G de Brevern1, Jean-Christophe Gelly1. 1. Inserm U1134, Paris, France, Université Paris Diderot, Sorbonne Paris Cité, UMR_S 1134, Paris, France, Institut National de la Transfusion Sanguine, Paris, France and Laboratory of Excellence GR-Ex, Paris, France.
Abstract
MOTIVATION: Template-based modeling, the most successful approach for predicting protein 3D structure, often requires detecting distant evolutionary relationships between the target sequence and proteins of known structure. Developed for this purpose, fold recognition methods use elaborate strategies to exploit evolutionary information, mainly by encoding amino acid sequence into profiles. Since protein structure is more conserved than sequence, the inclusion of structural information can improve the detection of remote homology. RESULTS: Here, we present ORION, a new fold recognition method based on the pairwise comparison of hybrid profiles that contain evolutionary information from both protein sequence and structure. Our method uses the 16-state structural alphabet Protein Blocks, which provides an accurate 1D description of protein structure local conformations. ORION systematically outperforms PSI-BLAST and HHsearch on several benchmarks, including target sequences from the modeling competitions CASP8, 9 and 10, and detects ∼10% more templates at fold and superfamily SCOP levels. AVAILABILITY: Software freely available for download at http://www.dsimb.inserm.fr/orion/. CONTACT: jean-christophe.gelly@univ-paris-diderot.fr. SUPPLEMENTARY INFORMATION: Supplementary data are available at Bioinformatics online.
MOTIVATION: Template-based modeling, the most successful approach for predicting protein 3D structure, often requires detecting distant evolutionary relationships between the target sequence and proteins of known structure. Developed for this purpose, fold recognition methods use elaborate strategies to exploit evolutionary information, mainly by encoding amino acid sequence into profiles. Since protein structure is more conserved than sequence, the inclusion of structural information can improve the detection of remote homology. RESULTS: Here, we present ORION, a new fold recognition method based on the pairwise comparison of hybrid profiles that contain evolutionary information from both protein sequence and structure. Our method uses the 16-state structural alphabet Protein Blocks, which provides an accurate 1D description of protein structure local conformations. ORION systematically outperforms PSI-BLAST and HHsearch on several benchmarks, including target sequences from the modeling competitions CASP8, 9 and 10, and detects ∼10% more templates at fold and superfamily SCOP levels. AVAILABILITY: Software freely available for download at http://www.dsimb.inserm.fr/orion/. CONTACT: jean-christophe.gelly@univ-paris-diderot.fr. SUPPLEMENTARY INFORMATION: Supplementary data are available at Bioinformatics online.
Authors: Jonathan Barnoud; Hubert Santuz; Alexandre G de Brevern; Pierre Poulain; Pierrick Craveur; Agnel Praveen Joseph; Vincent Jallu Journal: PeerJ Date: 2017-11-20 Impact factor: 2.984