Our projects

MYOSINOME DATABASE Myosinome

Myosins are one of the largest protein superfamilies with 24 classes. They have conserved structural features and catalytic domains yet show huge variation at different domains resulting in a variety of functions. Myosins are molecules driving various kinds of cellular processes and motility until the level of organisms. These are ATPases that utilize the chemical energy released by ATP hydrolysis to bring about conformational changes leading to a motor function. Myosins are important as they are involved in almost all cellular activities ranging from cell division to transcriptional regulation. They are crucial due to their involvement in many congenital diseases symptomatized by muscular malfunctions, cardiac diseases, deafness, neural and immunological dysfunction, and so on, many of which lead to death at an early age.  We present Myosinome, a database of selected myosin classes (myosin II, V, and VI) from five model organisms. This knowledge base provides the sequences, phylogenetic clustering, domain architectures of myosins and molecular models, structural analyses, and relevant literature of their coiled-coil domains. 

DATABASE OF OLFACTORY RECEPTOR

DOR is a database that provides sequence and structural information on olfactory receptors (OR) of selected organisms (Saccharomyces cerevisiae, Drosophila melanogaster, Caenorhabditis elegans, Mus musculus and Homo sapiens). Olfactory receptors are membrane proteins which help organisms to detect, encode, and process sensory stimuli. DOR provides users with olfactory receptor sequences for retrieval, predicted membrane topology, intra and inter-genomic alignments, phylogeny and identify motifs. The database contains three-dimensional structures of 100 selected ORs, modeled using bovine rhodopsin as template. The user can browse through the alignment used for comparative modeling of the olfactory receptors, structural models of the receptors, analyse the transmembrane regions marked on the model and the predicted dimer interface of every model.

DOSA: Database of Structural Alignments

Protein structure alignment is a crucial step in protein structure–function analysis. Despite the advances in protein structure alignment algorithms, some of the local conformationally similar regions are mislabeled as structurally variable regions (SVRs). These regions are not well superimposed because of differences in their spatial orientations. The Database of Structural Alignments (DoSA) addresses this gap in identification of local structural similarities obscured in global protein structural alignments by realigning SVRs using an algorithm based on protein blocks. A set of protein blocks is a structural alphabet that abstracts protein structures into 16 unique local structural motifs. DoSA provides unique information about 159 780 conformationally similar and 56 140 conformationally dissimilar SVRs in 74 705 pairwise structural alignments of homologous proteins. 

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