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Curr Opin Struct Biol. 2011 Aug;21(4):567-72. doi: 10.1016/j.sbi.2011.06.011. Epub 2011 Jul 21.

Nanobody stabilization of G protein-coupled receptor conformational states.

Author information

1
Department of Molecular and Cellular Interactions, Vlaams Instituut voor Biotechnologie & Structural Biology Brussels, Vrije Universiteit Brussel, Pleinlaan 2, B-1050 Brussels, Belgium. Jan.Steyaert@vib-vub.be

Abstract

Remarkable progress has been made in the field of G protein-coupled receptor (GPCR) structural biology during the past four years. Several obstacles to generating diffraction quality crystals of GPCRs have been overcome by combining innovative methods ranging from protein engineering to lipid-based screens and microdiffraction technology. The initial GPCR structures represent energetically stable inactive-state conformations. However, GPCRs signal through different G protein isoforms or G protein-independent effectors upon ligand binding suggesting the existence of multiple ligand-specific active states. These active-state conformations are unstable in the absence of specific cytosolic signaling partners representing new challenges for structural biology. Camelid single chain antibody fragments (nanobodies) show promise for stabilizing active GPCR conformations and as chaperones for crystallogenesis.

PMID:
21782416
PMCID:
PMC3166880
DOI:
10.1016/j.sbi.2011.06.011
[Indexed for MEDLINE]
Free PMC Article

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