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Volume 2, Issue 3, Pages 209-219 (March 1994) Structures of a legume lectin complexed with the human lactotransferrin N2 fragment, and with an isolated biantennary glycopeptide: role of the fucose moiety Yves Bourne, Joël Mazurier, Dominique Legrand, Pierre Rougé, Jean Montreuil, Geneviève Spik, Christian Cambillau Structure Volume 2, Issue 3, Pages 209-219 (March 1994) DOI: 10.1016/S0969-2126(00)00022-8

Figure 1 Structure of the glycopeptide isolated from human lactotransferrin [14]. Boxed parts indicate the heterogeneity of the sugar. Human lactotransferrin has two different N- glycosylation sites: Asn137 in the N-lobe and Asn478 in the C- lobe [12]. The biantennary octasaccharide previously used in the LOL I–octasaccharide complex [8] comprises the sugars numbered 2, 3, 4, 5, 6 and 4′ , 5′, 6′ in the structure shown here. NeuAc = N-acetylneuraminic acid, Gal = galactose, GlcNAc = N-acetylglucosamine, Man = mannose, Fuc = fucose. Structure 1994 2, 209-219DOI: (10.1016/S0969-2126(00)00022-8)

Figure 2 Ribbon diagram of the LOL II–N2 structure. (a)Since the asymmetric unit of these crystals contains only one monomer of LOL II and one N2 fragment, the second unit of these crystals contains only one monomer of LOL II and one N2 fragment, the second half of LOL II with the bound N2 fragment was generated around a crystallographic axis. (b)Close-up of the interaction between LOL II and fragment N2. The oligosaccharide (purple) is shown in the space-filling mode with Man- 4and Fuc- 1′(green). Residue Gln110 of fragment N2 (dark red) stabilizes GlcNAc- 1. Hydrophobic residues (Phe123 and Tyr77) of LOL II are shown (pale green). In the proteins, β -sheets are shown as blue arrows, α -helices as red cylinders and other regions are yellow. For clarity, the Fe 3+ion (brown) has been added at the bottom of helix 5 in the N2 fragment (although it is actually absent from the complex.) Structure 1994 2, 209-219DOI: (10.1016/S0969-2126(00)00022-8)

Figure 2 Ribbon diagram of the LOL II–N2 structure. (a)Since the asymmetric unit of these crystals contains only one monomer of LOL II and one N2 fragment, the second unit of these crystals contains only one monomer of LOL II and one N2 fragment, the second half of LOL II with the bound N2 fragment was generated around a crystallographic axis. (b)Close-up of the interaction between LOL II and fragment N2. The oligosaccharide (purple) is shown in the space-filling mode with Man- 4and Fuc- 1′(green). Residue Gln110 of fragment N2 (dark red) stabilizes GlcNAc- 1. Hydrophobic residues (Phe123 and Tyr77) of LOL II are shown (pale green). In the proteins, β -sheets are shown as blue arrows, α -helices as red cylinders and other regions are yellow. For clarity, the Fe 3+ion (brown) has been added at the bottom of helix 5 in the N2 fragment (although it is actually absent from the complex.) Structure 1994 2, 209-219DOI: (10.1016/S0969-2126(00)00022-8)

Figure 3 Close-up stereoviews of the 2F o–F celectron density map. (a)The glycopeptide in site C based on the final model of LOL II–glycopeptide structure. (b)The oligosaccharide linked to N2-Asn137 in the final model of LOL II–N2 structure. Residue Gln110 is shown hydrogen-bound to the N-acetyl group of GlcNAc- 1. Both maps are contoured at 0.9 σ. Structure 1994 2, 209-219DOI: (10.1016/S0969-2126(00)00022-8)

Figure 3 Close-up stereoviews of the 2F o–F celectron density map. (a)The glycopeptide in site C based on the final model of LOL II–glycopeptide structure. (b)The oligosaccharide linked to N2-Asn137 in the final model of LOL II–N2 structure. Residue Gln110 is shown hydrogen-bound to the N-acetyl group of GlcNAc- 1. Both maps are contoured at 0.9 σ. Structure 1994 2, 209-219DOI: (10.1016/S0969-2126(00)00022-8)

Figure 4 Superposition in stereo of (a) the oligosaccharide structures present in the LOL II–N2 (thick line) and LOL II–glycopeptide (thin line) structures and (b) the three glycopeptides present in the LOL II–glycopeptide structure. Thin, medium and bold lines represent the glycan in site A, B and C, respectively. Structure 1994 2, 209-219DOI: (10.1016/S0969-2126(00)00022-8)

Figure 4 Superposition in stereo of (a) the oligosaccharide structures present in the LOL II–N2 (thick line) and LOL II–glycopeptide (thin line) structures and (b) the three glycopeptides present in the LOL II–glycopeptide structure. Thin, medium and bold lines represent the glycan in site A, B and C, respectively. Structure 1994 2, 209-219DOI: (10.1016/S0969-2126(00)00022-8)

Figure 5 Stereoview of lectin–glycopeptide interactions in the LOL II–glycopeptide structure. For clarity, residues of the monosaccharide-binding site have been omitted. Structure 1994 2, 209-219DOI: (10.1016/S0969-2126(00)00022-8)

Figure 6 Superposition in stereo of the octasaccharide parts present in the LOL II–glycopeptide (thick line) and LOL I– octasaccharide (thin line) structures on the basis of Man- 4and GlcNAc- 5. Structure 1994 2, 209-219DOI: (10.1016/S0969-2126(00)00022-8)

Figure 7 Stereoview of the LOL II oligosac charide-binding site after superposition of the equivalent Cα atoms between LOL II (thin line) and ConA (thick line). Steric clashes between His205 of ConA and Fuc- 1′are clearly visible. Tyr12, Leu99, Ser168 and His205 of ConA coincide with Phe123, Ala210, Asn39 and Asn78 of LOL II. Structure 1994 2, 209-219DOI: (10.1016/S0969-2126(00)00022-8)