ABSTRACT
Allergy poses major health problems in industrialized countries, affecting over 20% of the population. Proteins from transgenic foods, cosmetics, animal hair, and other ubiquitous sources can be allergens. For this reason, development of improved methods for the prediction of potential allergenicity of proteins is timely. The currently available approaches to allergenicity prediction are numerous. Some approaches relied heavily on information on protein three-dimensional (3D) structure for allergenicity prediction. They required knowledge about 3D structure of query protein, thereby considerably restricting analysis to only those proteins whose 3D structure was known. As a consequence, many proteins with unknown structure could be overlooked. We developed a new method for allergenicity prediction, using information on protein 3D structure only for training. Three-dimensional structures of known allergenic proteins were used for representing protein surface as patches designated as discontinuous peptides. Allergenicity was predicted through search of such peptides in query protein sequences. It was demonstrated that the information on the discontinuous peptides made feasible better prediction of allergenic proteins. The allergenicity prediction method is available at http://www-bionet.sscc.ru/psd/cgi-bin/programs/Allergen/allergen.cgi .
Subject(s)
Allergens/chemistry , Peptides/chemistry , Proteins/chemistry , Algorithms , Allergens/immunology , Hypersensitivity/immunology , Peptides/immunology , Protein Conformation , Proteins/immunologyABSTRACT
WebProAnalyst is a web-accessible analysis tool (http://wwwmgs.bionet.nsc.ru/mgs/programs/panalyst/) designed for scanning quantitative structure-activity relationships in protein families. The tool allows users to search correlations between protein activity and physicochemical characteristics (i.e. hydrophobicity or alpha-helical amphipathicity) in queried sequences. WebProAnalyst uses aligned amino acid sequences and data on protein activity (pK, K(m), ED(50), among others). WebProAnalyst implements methods of the known ProAnalyst package, including the multiple linear regression analysis and the sequence-activity correlation coefficient. In addition, WebProAnalyst incorporates a method based on neural networks. The WebProAnalyst reports a list of sites in protein family, the regression analysis parameters (including correlation values) for the relationships between the amino acid physicochemical characteristics in the site and the protein activity values. WebProAnalyst is useful in search of the amino acid residues that are important for protein function/activity. Furthermore, WebProAnalyst may be helpful in designing the protein-engineering experiments.
Subject(s)
Proteins/chemistry , Proteins/metabolism , Software , Antimicrobial Cationic Peptides/chemistry , Antimicrobial Cationic Peptides/metabolism , Internet , Proteins/classification , Quantitative Structure-Activity Relationship , Viral Matrix Proteins/chemistry , Viral Matrix Proteins/metabolismABSTRACT
The PDBSite database provides comprehensive structural and functional information on various protein sites (post-translational modification, catalytic active, organic and inorganic ligand binding, protein-protein, protein-DNA and protein-RNA interactions) in the Protein Data Bank (PDB). The PDBSite is available online at http://wwwmgs.bionet.nsc.ru/mgs/gnw/pdbsite/. It consists of functional sites extracted from PDB using the SITE records and of an additional set containing the protein interaction sites inferred from the contact residues in heterocomplexes. The PDBSite was set up by automated processing of the PDB. The PDBSite database can be queried through the functional description and the structural characteristics of the site and its environment. The PDBSite is integrated with the PDBSiteScan tool allowing structural comparisons of a protein against the functional sites. The PDBSite enables the recognition of functional sites in protein tertiary structures, providing annotation of function through structure. The PDBSite is updated after each new PDB release.
Subject(s)
Databases, Protein , Models, Molecular , Proteins/chemistry , Binding Sites , Humans , Mutation , Protein Structure, Tertiary , Proteins/genetics , Proteins/metabolism , Software , Tumor Suppressor Protein p53/chemistryABSTRACT
PDBSiteScan is a web-accessible program designed for searching three-dimensional (3D) protein fragments similar in structure to known active, binding and posttranslational modification sites. A collection of known sites we designated as PDBSite was set up by automated processing of the PDB database using the data on site localization in the SITE field. Additionally, protein-protein interaction sites were generated by analysis of atom coordinates in heterocomplexes. The total number of collected sites was more than 8100; they were assigned to more than 80 functional groups. PDBSiteScan provides automated search of the 3D protein fragments whose maximum distance mismatch (MDM) between N, Calpha and C atoms in a fragment and a functional site is not larger than the MDM threshold defined by the user. PDBSiteScan requires perfect matching of amino acids. PDBSiteScan enables recognition of functional sites in tertiary structures of proteins and allows proteins with functional information to be annotated. The program PDBSiteScan is available at http://wwwmgs.bionet.nsc.ru/mgs/systems/fastprot/pdbsitescan.html.
