Bimolecular fluorescence complementation in structural biology.
Bimolecular fluorescence complementation is a method of probing protein-ligand interactions under physiological conditions. It provides a state-of-the-art tool to examine interactions observed in 3D structures of multi-component protein complexes, either to validate new experimental structures or to assess the correctness of homology models. Applications of the method range from homo- and hetero-oligomeric assemblies, including non-protein-ligands. Proof-of-principle experiments have also shown the potential of bimolecular fluorescence complementation to monitor protein complexes in a conformation-dependent manner. Here, recent highlights of structure-based applications of the method are outlined and assessed in terms of project-specific findings. These examples demonstrate the power of bimolecular fluorescence complementation to become a leading analysis tool in structural biology, to independently evaluate and characterize higher-order protein complexes.
Song
Young-Hwa
YH
EMBL-Hamburg, Notkestrasse 85, D-22603 Hamburg, Germany. song@embl-hamburg.de
Wilmanns
Matthias
M
D000818:Animals; D036022:Capsid Proteins / Q000032:analysis* / Q000235:genetics / Q000378:metabolism*; D005456:Fluorescent Dyes / Q000032:analysis / Q000378:metabolism; D005822:Genetic Vectors; D006801:Humans; D008164:Luminescent Proteins / Q000032:analysis* / Q000235:genetics / Q000378:metabolism; D008840:Microfilament Proteins / Q000032:analysis* / Q000235:genetics / Q000378:metabolism*; D008856:Microscopy, Fluorescence / Q000379:methods*; D010957:Plasmids; D025941:Protein Interaction Mapping / Q000379:methods; D055503:Protein Multimerization; D011993:Recombinant Fusion Proteins / Q000032:analysis / Q000378:metabolism / Q000528:radiation effects; D040681:Structural Homology, Protein; D014162:Transfection
D036022:Capsid Proteins; D005456:Fluorescent Dyes; D008164:Luminescent Proteins; D008840:Microfilament Proteins; D011993:Recombinant Fusion Proteins