Shubhra Ghosh Dastidar

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Tubulin, an α,β heterodimer, has four distinct ligand binding sites (for paclitaxel, peloruside/laulimalide, vinca, and colchicine). The site where colchicine binds is a promising drug target for arresting cell division and has been observed to accommodate compounds that are structurally diverse but possess comparable affinity. This investigation, using two(More)
Over the last few decades Cry1Ac toxin has been widely used in controlling the insect attack due to its high specificity towards target insects. The pore-forming toxin undergoes a complex mechanism in the insect midgut involving sequential interaction with specific glycosylated receptors in which terminal GalNAc molecule plays a vital role. Recent studies(More)
The basic framework of understanding the mechanisms of protein functions is achieved from the knowledge of their structures which can model the molecular recognition. Recent advancement in the structural biology has revealed that in spite of the availability of the structural data, it is nontrivial to predict the mechanism of the molecular recognition which(More)
The Bcl-xl protein is a potential drug target for cancer, and it has a relatively flat and flexible binding pocket. ABT263 is one of the most promising molecules that inhibit Bcl-xl, and it was developed from its precursor ABT737 with suitable substitutions. However, the structural and mechanistic implications of those changes have not yet been reported.(More)
Bcl-xL, a member of the Bcl-2 family of proteins, remains distributed over the cytosol and the mitochondrial membrane, maintaining a balance between apoptosis and the survival of the cell. Passage to the membrane is essential for its biological functions (e.g. to antagonize pro-apoptotic proteins of the Bcl2 family), which is known to be initiated by the(More)
The dynamic instability of the microtubule originates from the conformational switching of its building block, that is, the α, β-tubulin dimer. Ligands occupying the interface of the α-β dimer bias the switch toward the disintegration of the microtubule, which in turn controls the cell division. A little loop of tubulin is structurally encoded as a(More)
Bcl-xl protein has a long unstructured loop attached to its structured region which joins two helices. The necessity to have this unstructured segment in Bcl-xl is not yet well understood. To what extent the unstructured segment can influence the dynamics of the structured region of protein, with potential to influence the function, has been investigated in(More)
The interaction between the ribosome and the endoplasmic reticulum-located Sec61 protein translocon is mediated through an arginine residue of Sec61α, which is conserved in all prokaryotic and eukaryotic orthologues characterized to date. Using in silico approaches we report that instead of arginine, this ribosome-interaction function is most likely(More)
TN16 is one of the most promising inhibitors of α, β dimer of tubulin that occupies the cavity in the β-subunit located at the dimeric interface, known as the colchicine binding site. The experimentally determined structure of the complex (Protein Data Bank entry 3HKD) presents the conformation and position of the ligand based on the "best fit", keeping the(More)
The Bcl2 family of proteins is capable of switching the apoptotic machinery by directly controlling the release of apoptotic factors from the mitochondrial outer membrane. They have 'pro' and 'anti'-apoptotic subgroups of proteins which antagonize each other's function; however a detailed atomistic understanding of their mechanisms based on the dynamical(More)
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