What is it about?
Cell-surface receptors control multiple cellular functions and are attractive targets for drug design. These receptors often have dedicated extracellular domains that bind signaling molecules, such as hormones and nutrients. Computational identification of these ligand-binding domains in genomic sequences is a pre-requisite for their further experimental characterization. Using available three-dimensional structures of several bacterial cell-surface receptors, we built computational models that enabled identification of the Cache domain.
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Why is it important?
We found that Cache domain is the most common extracellular sensor module in prokaryotes, including many important pathogens. We also demonstrated that the Cache domain is homologous to, but sufficiently different from the most common intracellular sensor module, the PAS domain. These findings provide a unified view on molecular principles of signal recognition by extra- and intracellular receptors.
Perspectives
With this study, Cache domains are meticulously characterized. Evolutionary history of the superfamily enabled us to understand their origin and current landscape. We resolved some discrepancies between Cache domain models that were previously built based on structure and sequence. Our newly defined Cache domain models now exist in the PFAM database.
Ogun Adebali
American Diplomacy Publishers
Read the Original
This page is a summary of: Cache Domains That are Homologous to, but Different from PAS Domains Comprise the Largest Superfamily of Extracellular Sensors in Prokaryotes, PLoS Computational Biology, April 2016, PLOS,
DOI: 10.1371/journal.pcbi.1004862.
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