Prof. Dr. Karl-Wilhelm Koch
Office: W4 1-137
Neuronal calcium sensor (NCS) proteins constitute a family of proteins, which can be further subdivided into five subfamilies. A common feature of NCS proteins is the presence of 4 EF-hand motifs (calcium binding region), which consist of a loop region (12 amino acids) that is flanked by two a-helices (see figure). Almost all NCS proteins harbour at the N-terminus a consensus site for cotranslational myristoylation. Prototype of the NCS protein family is recoverin that is mainly expressed in the vertebrate retina. Another subfamily contains the GCAPs (guanylate cyclase-activating proteins) that regulate the activities of membrane bound guanylate cyclases in the vertebrate retina.
Scholten, A. and Koch, K.-W. (2011) Differential calcium signaling by cone specific guanylate cyclase-activating proteins from the zebrafish retina. PLoS One; 6(8): e23117. doi:10.1371/journal.phone.0023117
Wache, N., Scholten, A., Klüner T., Koch, K.-W. and Christoffers, J. (2012) Turning on fluorescence with thiols - synthetic and computational studies on diaminoterephthalates and monitoring the switch of the Ca2+ sensor recoverin. Eur. J. Org. Chem. 2012, 5712-5722.
Robin, J., Brauer, J., Sulmann, S., Marino, V., Dell’Orco, D., Lienau, C., and Koch, K.-W. (2015) Differential nanosecond protein dynamics in homologous calcium sensors. ACS Chem. Biol. 10, 2344–2352.
Sulmann, S., Kussrow, A., Bornhop, D.J. and Koch, K.-W. (2017) Label-free quantification of calcium-sensor targeting to photoreceptor guanylate cyclase and rhodopsin kinase by backscattering interferometry. Sci. Rep. 7:45515.
Abbas, S., Marino, V., Dell'Orco, D., and Koch, K.-W. (2019) Molecular Recognition of Rhodopsin Kinase GRK1 and Recoverin Is Tuned by Switching Intra- and Intermolecular Electrostatic Interactions. Biochemistry 58, 4374-4385.
Marino, V., Riva, M., Zamboni, D., Koch, K.-W. and Dell'Orco, D. (2021) Bringing the Ca2+ sensitivity of myristoylated recoverin into the physiological range. Open Biol. 11(1):200346. doi: 10.1098/rsob.200346.