Title | Nanobody stabilization of G protein-coupled receptor conformational states. |
Publication Type | Journal Article |
Year of Publication | 2011 |
Authors | Steyaert, J., and B. K. Kobilka |
Journal | Curr Opin Struct Biol |
Volume | 21 |
Issue | 4 |
Pagination | 567-72 |
Date Published | 2011 Aug |
ISSN | 1879-033X |
Keywords | Animals, Crystallography, X-Ray, Humans, Immunoglobulin Fragments, Protein Conformation, Protein Stability, Receptors, G-Protein-Coupled, Single-Chain Antibodies |
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. |
DOI | 10.1016/j.sbi.2011.06.011 |
Alternate Journal | Curr. Opin. Struct. Biol. |
PubMed ID | 21782416 |
PubMed Central ID | PMC3166880 |
Grant List | GM083118 / GM / NIGMS NIH HHS / United States NS028471 / NS / NINDS NIH HHS / United States R01 GM083118 / GM / NIGMS NIH HHS / United States R01 GM083118-03 / GM / NIGMS NIH HHS / United States R01 GM083118-04 / GM / NIGMS NIH HHS / United States R37 NS028471 / NS / NINDS NIH HHS / United States R37 NS028471-20 / NS / NINDS NIH HHS / United States |
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