Identifying ligand-binding hot spots in proteins using brominated fragments.
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ABSTRACT:
SUBMITTER: Groftehauge MK
PROVIDER: S-EPMC3758163 | biostudies-literature | 2013 Sep
REPOSITORIES: biostudies-literature
Publications
Identifying ligand-binding hot spots in proteins using brominated fragments.
Grøftehauge Morten K MK Therkelsen Martin Ø MØ Taaning Rolf R Skrydstrup Troels T Morth J Preben JP Nissen Poul P
Acta crystallographica. Section F, Structural biology and crystallization communications 20130819 Pt 9
High-quality crystals of Thermus thermophilus EF-Tu in the GTP-bound conformation at 1.7-2.7 Å resolution were used to test 18 small organic molecules, all brominated for confident identification in the anomalous difference maps. From this relatively small collection, it was possible to identify a small molecule bound in the functionally important tRNA CCA-end binding pocket. The antibiotic GE2270 A is known to interact with the same pocket in EF-Tu and to disrupt the association with tRNA. Brom ...[more]
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