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TitleOn the Importance of Carbohydrate-Aromatic Interactions for the Molecular Recognition of Oligosaccharides by Proteins: NMR Studies of the Structure and Binding Affinity of AcAMP2-like Peptides with Non-Natural Naphthyl and Fluoroaromatic Residues
Journal, issue, pagesChemistry, Vol. 11, Page 7060-7074, Year 2005
Publish dateMay 12, 2005 (structure data deposition date)
AuthorsChavez, M.I. / Andreu, C. / Vidal, P. / Aboitiz, N. / Freire, F. / Groves, P. / Asensio, J.L. / Asensio, G. / Muraki, M. / Canada, F.J. / Jimenez-Barbero, J.
External linksChemistry / PubMed:16220560
MethodsNMR (solution)
Structure data

PDB-1znt:
18 NMR structures of AcAMP2-Like Peptide with non Natural Fluoroaromatic Residue (AcAMP2F18Pff/Y20Pff) complex with N,N,N-triacetylchitotriose
Method: SOLUTION NMR

PDB-1zuv:
24 NMR structures of AcAMP2-Like Peptide with Phenylalanine 18 mutated to Tryptophan
Method: SOLUTION NMR

PDB-1zwu:
30 NMR structures of AcAMP2-like peptide with non natural beta-(2-naphthyl)-alanine residue.
Method: SOLUTION NMR

KeywordsANTIMICROBIAL PROTEIN / alfa-helix / anti-parallel beta-sheet / alpha-helix / anti-parallel beta-sheet.

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