Home > Academics > Academic Units > Schools > Bio Science > Dibyendu Samanta
Assistant Professor Grade-I
Bio Science
Dr. Dibyendu Samanta's laboratory focuses on structure-function relationship of membrane proteins, particularly membrane-bound immunoglobulin super-family (IgSF) members. These IgSFs play vital roles in a number of cellular and physiological processes including cell-cell adhesion, immune modulation, host-pathogen interaction etc. Dr. Samanta's lab aims to understand the detail molecular mechanisms of interactions among IgSF members, and finally modulate these interactions utilizing structure-guided protein engineering approach. Understanding and engineering of these IgSF members will provide further insights for the development of novel protein-based therapeutics. Currently, Dr. Samant's lab working on the following areas:
1. Structrure-function relationships of cell adhesion molecules: cadherin and nectin
2. Molecular and structural bases of function involving immunoglobulin-superfamily (IgSF) members.
3. Protein engineering to study protein-protein interactions
Molecular and structural bases of interaction between extracellular domains of nectin-2 and N-cadherin. by Duraivelan K., Basak A. J., Ghosh A. , Samanta D. Proteins 86 1157-1164 (2018)
Genetically modified hematopoietic stem/progenitor cells that produce IL-10-secreting regulatory T cells. by Ng S. L., Leno-duran E. , Samanta D. , Almo S. C., Strominger J. L. Proc Natl Acad Sci USA 116(7):2634-2639. 2634-2639 (2019)
Structural, mutational and biophysical studies reveal a canonical mode of molecular recognition between immune receptor TIGIT and nectin-2. by Samanta D., Guo H. , Rubinstein R. , Ramagopal U. , Almo S. Mol Immunol 81 151-159 (2017)
Nectin family of cell-adhesion molecules: structural and molecular aspects of function and specificity by Samanta D., Almo S. Cell Mol Life Sci 72 645-658 (2015)
Structure of Nectin-2 reveals determinants of homophilic and heterophilic interactions that control cell-cell adhesion by Samanta D, Ramagopal UA, Rubinstein R, Vladimir V, Nathenson SG, Almo SC Proc Natl Acad Sci USA 109 14836-14840 (2012)
Identical RNA-protein interactions in vivo and in vitro and a scheme of folding the newly synthesized proteins by ribosomes. by Das D., Samanta D. , Hassan S. , Das A. , Bhattacharyay A. , Dasgupta S. , Chakrabarti A. , Ghorai P. , Dasgupta C. J Biol Chem 287 37508-37521 (2012)
Structural and Functional Characterization of a Single-chain Peptide-MHC Molecule that Modulates Both Naive and Activated CD8+ T Cells by Samanta D*, Mukherjee G*, Ramagopal UA, Chaparro RJ, Nathenson SG, DiLorenzo TP, Almo SC. (*equally contributed) Proc Natl Acad Sci USA 108 13682-13687 (2011)
Mechanism of ribosome assisted protein folding: a new insight into rRNA functions by Samanta D*, Das A, Bhattacharya A, Basu A, Das D, DasGupta C*. (*corresponding author) Biochem Biophys Res Commun 384 137-140 (2009)
Protein folding following synthesis in vitro and in vivo: association of newly synthesized protein with 50S subunit of E. coli ribosome by Basu A*, Samanta D*, Bhattacharya A, Das A, Das D, Dasgupta C. (*equally contributed) Biochem Biophys Res Commun 366 592-597 (2008)
Protein folding by domain V of Escherichia coli 23S rRNA: specificity of RNA-protein interactions by Samanta D, Mukhopadhyay D, Chowdhury S, Ghosh J, Pal S, Basu A, Bhattacharya A, Das A, Das D, DasGupta C J Bacteriol 190 3344-3352 (2008)
Molecular and Structural Studies of the Role of Host Adhesion Molecules in Facilitating LpqH (19 kDa Surface Antigen) Mediated Entry of Mycobacterium Tuberculosis into Pneumocytes MHRD-STARS
BTNL2, a Novel T Cell Coinhibitory Molecule, as a Therapeutic Target in Ulcerative Colitis DBT, NEW DELHI
Kheerthana D
Area of Research: Protein structure-function relationship and engineering
Bidisha Acharya
Area of Research: Regulation of HOX transcription factors
Aditya Jyoti Basak
Area of Research: Structure-function Relation of Membrane Proteins/Cell Adhesion Molecules
Shruti Chatterjee
Area of Research:
Sagarika Dash
Area of Research: structure-function relationship of membrane proteins
