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Jan Steyaert

VIB-VUB Center for Structural Biology, BE
Biography

Jan Steyaert ir. Ph.D. is a full professor and Francqui Research Professor at the Vrije Universiteit Brussel (VUB). He teaches biochemistry and protein engineering for chemists, biologists and bio-engineers.

Jan Steyaert made his Ph.D. at the protein engineering department of Plant Genetic Systems (currently Bayer Crop science). After a postdoc in the International Livestock Research Institute (Nairobi, Kenya), he joined the laboratory of Structural Biology of Lode Wyns. Skilled in enzymology, structural biology and antibody technology. Experienced in steady state and pre-steady state kinetics, protein expression and purification, spectroscopic techniques, structural biology methods and phage display. He is co-founder of Ablynx (www.ablynx.com) and Biotalys (www.biotalys.com), and founder of ConFo Therapeutics (www.confotherapeutics.com), three biotech spin-offs that valorize a unique family of single domain antibodies (nanobodies®) derived from camels.

Last years, the Steyaert lab pioneered the use of nanobodies® for chaperone-assisted X-ray crystallography (www.steyaertlab.eu), aiming at the highest hanging fruits of structural biology including membrane proteins, amyloidogenic proteins, and now also (transient) multiprotein complexes. The elucidation of the first GPCR structures in the agonist-bound active state demonstrate the power of Nanobodies® to stabilize G protein coupled receptor conformational states including transmembrane signalling complexes. Recent work focusses on exploiting the conformational complexity of therapeutic targets for Nanobody-enabled drug discovery.

Jan Steyaert holds a Ph.D in Bioengineering Sciences from the VUB. He is currently Director of the Structural Biology Brussels lab (VUB), Director and group leader of the Structural Biology Research center of the Vlaams Instituut voor Biotechnologie (VIB) and senior advisor of Confotherapeutics.

Representative publications:

  • Rostislavleva, K., et al. (2015). "Structure and flexibility of the endosomal Vps34 complex reveals the basis of its function on membranes." Science 350: aac7365.
  • Huang, W., et al. (2015). "Structural insights into micro-opioid receptor activation." Nature 524: 315-321.
  • Irannejad, R., et al. (2013). "Conformational biosensors reveal GPCR signalling from endosomes." Nature 495: 534-538.
  • Rasmussen, S. G., et al. (2011). "Crystal structure of the b2 adrenergic receptor-Gs protein complex." Nature 477: 549-555.

Rasmussen, S. G., et al. (2011). "Structure of a nanobody-stabilized active state of the b2 adrenoceptor." Nature 469: 175-180.

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