In-silico structural analysis of E509K mutation in LARGE and T192M mutation in Alpha Dystroglycan in the inhibition of glycosylation of Alpha Dystroglycan by LARGE.

Impaired glycosylation of cellular receptor Alpha Dystroglycan (α-DG) leads to dystroglycanopathy. Glycoprotein α-DG is the receptor protein in the Dystrophin Associated Protein Complex (DAPC), a macromolecular gathering on muscle cell membrane to form a bridge between extracellular matrix (ECM) and cellular actin cytoskeleton. Proper glycosylation of α-DG is mediated by the glycosylating enzyme LARGE.

Computational analyses of the length and compositional variations of the FNBP4 gene across 10 different species.

Formin binding protein 4 (FNBP4) interacts with formins and other proteins via its WW domains. Previously, we reported the structural and phylogenetic clustering of FNBP4 across a wide range of organisms from different taxonomic groups along with characterizing its plant variant (Arabidopsis thaliana F4JC80). Recently, the FNBP4 gene is reported to be associated with a congenital disorder Microphthalmia with Limb Anomalies.

Implication from the predicted docked interaction of sigma H and exploration of its interaction with RNA polymerase in Mycobacterium tuberculosis.

M. tuberculosis is adapted to remain active in the extreme environmental condition due to the presence of atypical sigma factors commonly called extra cytoplasmic function (ECF) sigma factors. Among the 13 sigma factors of M.

Analyses of the presence of mutations in Dystrophin protein to predict their relative influences in the onset of Duchenne Muscular Dystrophy.

Muscle plays a vital role in the life of vertebrates like humans. Muscle contraction is the only criterion required for locomotion. Muscle fibers also play a vital role as the provider of mechanical strength and act as a large repository of building blocks for protein synthesis in living beings.

In-silico characterization of Formin Binding Protein 4 Family of proteins.

Members of the Formin Binding Protein 4 Family or the FNBP4 were indirectly reported to be associated with many of the biological processes. These proteins possess two WW domains. So far there are practically no reports regarding the characterization and classification of the protein by any means.

Hypoglycosylation of dystroglycan due to T192M mutation: a molecular insight behind the fact.

Abnormal glycosylation of dystroglycan (DG), a transmembrane glycoprotein, results in a group of diseases known as dystroglycanopathy. A severe dystroglycanopathy known as the limb girdle disease MDDGC9 [OMIM: 613818] occurs as a result of hypoglycosylation of alpha subunit of DG. Reasons behind this has been traced back to a point mutation (T192M) in DG that leads to weakening of interactions of DG protein with laminin and subsequent loss of signal flow through the DG protein.