Our mission
We are a team of creative, ambitious and friendly researchers who investigate membrane transport processes in pathogenic bacteria and develop innovative protein engineering tools. We combine the disciplines of structural biology, binder generation, protein biochemistry and microbiology to uncover molecular details of how membrane transport proteins expel antibiotics, shuttle siderophores and export lipids. Sybodies and NestLink enable us to target membrane transporters in the cellular context to develop rapid diagnostics, novel antibiotics and tailor-made research tools.
Need to enlarge your sybodies? Try sybody-binding Fabs from @RapoportLab (Legobodies) and @lab_locher (NabFab) for bigger, better results! đź’ˇ https://t.co/nr9Jrm6wn1 & https://t.co/uNpZwSEAkT
Interested in using #sybodies for your research? No alpacas required 🦙. Reach out at https://t.co/dp38L7Zkm8. Thread by @f_ackle.
And one of our @seegerlab stories: Sybodies unlock crystal structure of ABC exporter TM287/288 đź’Ž. By binding to an extracellular wing, the sybody shifts the transporter's equilibrium, revealing the importance of gate closure. #ABCtransporter https://t.co/IbRUqiuIUC
Sybodies selected by @CamiloPerezC6H6 lab inhibit LicB, a key transporter in S. pneumoniae & bacterial pathogenesis🦠. Structures reveal distinct states & proton-coupled import. Uncovering insights to target the phosphocholine modification pathway. https://t.co/vm0WZVQocn https://t.co/a6PCBim9b4
Human GlyT1 structure unlocked by @PoulNissen lab! Using a sybody & serial synchrotron crystallography, researchers reveal how benzoylpiperazine inhibitors lock GlyT1 in an inward-open conformation, aiding CNS disorder therapies. 🧠💊 #Neuroscience https://t.co/UNTMs9kFg3 https://t.co/F4Y2cm5sob
Syb37 locks KDELR in apo state & reveals parts of its mechanism. By binding within the luminal cavity, it disrupts normal signal-mediated retrieval from Golgi, directing it to lysosomes. Syb37 was crucial for phasing KDELR structure. @inwardopen https://t.co/yyPf7wOezo https://t.co/zkuuPd5EIz
