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Frontispiece: Replacement of Water Molecules in a Phosphate Binding Site by Furanoside‐Appended lin ‐Benzoguanine Ligands of tRNA‐Guanine Transglycosylase (TGT)
Author(s) -
Barandun Luzi J.,
Ehrmann Frederik R.,
Zimmerli Daniel,
Immekus Florian,
Giroud Maude,
Grünenfelder Claudio,
Schweizer W. Bernd,
Bernet Bruno,
Betz Michael,
Heine Andreas,
Klebe Gerhard,
Diederich François
Publication year - 2015
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201580162
Subject(s) - moiety , chemistry , guanine , stereochemistry , ribose , transfer rna , nucleotide , anomer , phosphate , rna , biochemistry , enzyme , gene
Molecular Recognition In their Full Paper on page 126 ff., G. Klebe, F. Diederich et al. describe a novel series of lin ‐benzoguanines that target the polar ribose‐34 pocket of Z. mobilis TGT with a furanosyl moiety. The preparation involved a new cyclization strategy for the lin ‐benzoguanine core and the highly challenging separation of the anomeric mixtures by HPLC on a chiral stationary phase. They were designed to replace a conserved water cluster and differ by the functional groups at C(2) and C(3) of the furanosyl moiety being either OH or OMe.