Similarity between Protein–Protein and Protein–Carbohydrate Interactions, Revealed by Two Crystal Structures of Lectins from the Roots of Pokeweed

Lectin-bound conformations and non-covalent interactions of glycomimetic analogs of thiochitobiose

“…This may indicate that hydrophobic interactions play a major role for binding to PAL compared to WGA. This is in agreement with the known binding regions from X-ray analysis of PAL 22 and WGA 23 in complexation with their natural ligands. For WGA complexed with di-N-acetylchitobiose, several 'binding points' were found.…”

Structural Studies of a Two-domain Chitinase from Streptomyces griseus HUT6037

“…Despite lacking apparent sequence similarity, the folds share the structurally invariant core with lysozymes of GH families 22, 23, and 24, and chitosanases of GH family 46. 17,18 The main components of the core are included in the helices C and F and a b-sheet composed of b1, b2, and b3 as defined, 19 corresponding to Ile154 to Val157, Tyr182 to Pro186, and Ile187 to Ser190, respectively, of CatD ChiC . However, these residues localized around the cleft are in fact not recognized as a b-sheet by the Define Secondary Structure of Proteins (DSSP) algorithm.…”

“…In the crystal structure of PL-D2 complexed with tri-N-acetylchitotriose, the ligand molecule is sandwiched by two neighboring domains from independent molecules related by a crystallographic symmetry. 19 The binding is predominantly retained by face-to-face contacts between pyranose rings and two surface-exposed aromatic residues and by at least two hydrogen bonds with side-chains of a strictly conserved serine residue and an aromatic residue (tyrosine or histidine). q and R values in both proteins are comparable to each other ( Table 3), indicating that the interaction between ChBD ChiC and the ligand observed in the simulation is tight, similar to PL-D2, although the ligand is not sandwiched like that in PL-D2.…”

“…The coordinates of the ligand were derived from a tri-Nacetylchitotriose bound in the chitin-binding site of PL-D2 (PDB code: 1ULM 19 ). The saccharide residues were named NAG1, 2, and 3 from the non-reducing end to the reducing end.…”

NMR and Modeling Studies of Protein–Carbohydrate Interactions: Synthesis, Three‐Dimensional Structure, and Recognition Properties of a Minimum Hevein Domain with Binding Affinity for Chitooligosaccharides

“…[33][34][35] The same set of interactions is common to complexes of WGA, [38][39][40] pseudohevein, [41] Ac-AMP2, [42] the UDA dimer, [43,44] and pokeweed lectin. [45] In this work we have truncated the C terminus of hevein to obtain a 32-residue peptide (which we call HEV32) by solidphase synthesis with three disulfide bonds in a similar pattern to Ac-AMP2, but with an approximately 50 % sequence homology to this small peptide (Scheme 1). Secondly, the thermodynamic parameters of HEV32 binding to N,N',N''-triacetylchitotriose, (GlcNAc) 3 , and N,N',N'',N''',N'''',N'''''-hexaacetylchitohexaose, (GlcNAc) 6 , have been determined by NMR and fluorescence measurements.…”