Molecular recognition forms the basis for all cellular events- from a simple bimolecular enzymatic reaction to the cascades of multimeric protein complex in cell signaling. Fundamental to the structure and function of a protein is its ‘domain’- a discrete, minimal modular entity that constitutes one of the basic physical and functional unit of the polypeptide. This protein domain can either serve as a protein docking/interaction site or an active enzymatic unit. With the emphasis on functional genomics, it is important to address what role does each of these domains play and how their potential functions can be regulated across molecular, cellular and tissue levels.

One of the several protein domains that our group first identified and characterised is a novel protein domain termed BCH domain which play important roles in regulating cell growth/death, differentiation, migration, and tissue/organ development. Based on the prototypical BNIP-2 and BPGAP1 proteins, we show that distinct BCH domains could act as key modulators for Rho and Ras small GTPases as well as their immediate regulators such as guanine nucleotide exchange factors and GTPase-activating proteins. Current effort is geared towards understanding how cells and tissues respond to the dynamic forces and geometry in the environment both under the influence of the BCH domain as a versatile regulatory scaffold domain. These effects will be examined under normal and pathological conditions such as in cancers, neurological disorders, skin and heart diseases.