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Synopsis Interdisciplinary collaborations are essential for addressing complex global challenges, yet forming and sustaining such teams is often hindered by institutional barriers, differences in discipline-specific languages, and cultural divides. Existing tools and platforms frequently fail to foster the deep, ongoing engagement necessary for successful interdisciplinary work. This paper proposes a novel web-based platform designed to stimulate and support interdisciplinary collaborations by integrating social media elements, such as user-friendly communication tools, algorithms for identifying and connecting individuals with complementary and unique skills, and smart suggestions for potential collaborators. The platform would facilitate building and maintaining the engagement of target users, and provide guardrails to engender community trust, with a goal to also tackle issues related to power dynamics, cultural differences, institutional structures, and varying levels of prestige or funding. By addressing these challenges, the proposed platform would enable and accelerate productive interdisciplinary research and collaborative ideation, and ultimately stimulate more innovative and effective solutions to complex scientific and societal problems. 

Abstract Tuberculosis (TB), caused by the pathogenMycobacterium tuberculosis, affects millions of people worldwide. Several TB drugs have lost efficacy due to emerging drug resistance and new anti‐TB targets are needed. Recent research suggests that indole‐3‐glycerol phosphate synthase (IGPS) inM. tuberculosis(MtIGPS) could be such a target. IGPS is a (β/α)₈‐barrel enzyme that catalyzes the conversion of 1‐(o‐carboxyphenylamino)‐1‐deoxyribulose 5’‐phosphate (CdRP) into indole‐glycerol‐phosphate (IGP) in the bacterial tryptophan biosynthetic pathway.M. tuberculosisover expresses the tryptophan pathway genes during an immune response and inhibition ofMtIGPS allows CD4 T‐cells to more effectively fight againstM. tuberculosis. Here we review the published data onMtIGPS expression, kinetics, mechanism, and inhibition. We also discussMtIGPS crystal structures and compare them to other IGPS structures to reveal potential structure‐function relationships of interest for the purposes of drug design and biocatalyst engineering.