6tv7
From Proteopedia
Crystal structure of rsGCaMP in the OFF state (illuminated)
Structural highlights
DiseaseCALM1_HUMAN The disease is caused by mutations affecting the gene represented in this entry. Mutations in CALM1 are the cause of CPVT4. The disease is caused by mutations affecting the gene represented in this entry. Mutations in CALM1 are the cause of LQT14. FunctionCALM1_HUMAN Calmodulin mediates the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Among the enzymes to be stimulated by the calmodulin-calcium complex are a number of protein kinases and phosphatases. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis (PubMed:16760425). Mediates calcium-dependent inactivation of CACNA1C (PubMed:26969752). Positively regulates calcium-activated potassium channel activity of KCNN2 (PubMed:27165696).[1] [2] [3] [4] Publication Abstract from PubMedReversibly photo-switchable proteins are essential for many super-resolution fluorescence microscopic and optoacoustic imaging methods. However, they have yet to be used as sensors that measure the distribution of specific analytes at the nanoscale or in the tissues of live animals. Here we constructed the prototype of a photo-switchable Ca(2+) sensor based on GCaMP5G that can be switched with 405/488-nm light and describe its molecular mechanisms at the structural level, including the importance of the interaction of the core barrel structure of the fluorescent protein with the Ca(2+) receptor moiety. We demonstrate super-resolution imaging of Ca(2+) concentration in cultured cells and optoacoustic Ca(2+) imaging in implanted tumor cells in mice under controlled Ca(2+) conditions. Finally, we show the generalizability of the concept by constructing examples of photo-switching maltose and dopamine sensors based on periplasmatic binding protein and G-protein-coupled receptor-based sensors. Genetically encoded photo-switchable molecular sensors for optoacoustic and super-resolution imaging.,Mishra K, Fuenzalida-Werner JP, Pennacchietti F, Janowski R, Chmyrov A, Huang Y, Zakian C, Klemm U, Testa I, Niessing D, Ntziachristos V, Stiel AC Nat Biotechnol. 2021 Nov 29. pii: 10.1038/s41587-021-01100-5. doi:, 10.1038/s41587-021-01100-5. PMID:34845372[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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