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   Related Articles
   [25]The domain-swapped dimer of cyanovirin-N contains two s...
   Biochemical and Biophysical Research Communications

   Close
   You are entitled to access the full text of this document  [26]The
   domain-swapped dimer of cyanovirin-N contains two sets of
   oligosaccharide binding sites in solution  Original Research Article
   Biochemical and Biophysical Research Communications, Volume 298, Issue
   4, 8 November 2002, Pages 598-602
   Laura G. Barrientos, Angela M. Gronenborn
   Abstract
   The binding of high-mannose oligosaccharides to the domain-swapped
   dimeric form of the potent HIV-inactivating protein cyanovirin-N (CV-N)
   was investigated in solution by NMR, complementing recent structural
   studies by X-ray crystallography on similar complexes [J. Biol. Chem.
   277 (2002) 34336]. The crystal structures of CV-N dimer complexed with
   Man-9 and hexamannoside revealed two carbohydrate binding sites on
   opposite ends of the molecule. No binding was observed at site 1,
   previously identified on the solution monomer of CV-N [Structure 9
   (2001) 931; Shenoy et al., Chem. Biol. 9 (2002) 1109]. Here, we report
   the presence of four sugar binding sites on the CV-N dimer in solution,
   identified by chemical shift mapping with hexamannoside and
   nonamannoside, synthetic substructures of Man-9. Our results