1Q8S
Pterocarpus angolensis lectin (PAL) in complex with the dimannoside Man(alpha1-6)Man
Summary for 1Q8S
Entry DOI | 10.2210/pdb1q8s/pdb |
Related | 1N3O 1N3P 1N3Q 1Q8O 1Q8P 1Q8Q 1Q8V 1UKG |
Descriptor | lectin, alpha-D-mannopyranose-(1-6)-methyl alpha-D-mannopyranoside, MANGANESE (II) ION, ... (5 entities in total) |
Functional Keywords | lectin, carbohydrate, mannose, sugar binding protein |
Biological source | Pterocarpus angolensis |
Total number of polymer chains | 2 |
Total formula weight | 56019.27 |
Authors | Loris, R.,Van Walle, I.,De Greve, H.,Beeckmans, S.,DeBoeck, F.,Wyns, L.,Bouckaert, J. (deposition date: 2003-08-22, release date: 2004-02-10, Last modification date: 2020-07-29) |
Primary citation | Loris, R.,Van Walle, I.,De Greve, H.,Beeckmans, S.,Deboeck, F.,Wyns, L.,Bouckaert, J. Structural Basis of Oligomannose Recognition by the Pterocarpus angolensis Seed Lectin J.Mol.Biol., 335:1227-1240, 2004 Cited by PubMed Abstract: The crystal structure of a Man/Glc-specific lectin from the seeds of the bloodwood tree (Pterocarpus angolensis), a leguminous plant from central Africa, has been determined in complex with mannose and five manno-oligosaccharides. The lectin contains a classical mannose-specificity loop, but its metal-binding loop resembles that of lectins of unrelated specificity from Ulex europaeus and Maackia amurensis. As a consequence, the interactions with mannose in the primary binding site are conserved, but details of carbohydrate-binding outside the primary binding site differ from those seen in the equivalent carbohydrate complexes of concanavalin A. These observations explain the differences in their respective fine specificity profiles for oligomannoses. While Man(alpha1-3)Man and Man(alpha1-3)[Man(alpha1-6)]Man bind to PAL in low-energy conformations identical with that of ConA, Man(alpha1-6)Man is required to adopt a different conformation. Man(alpha1-2)Man can bind only in a single binding mode, in sharp contrast to ConA, which creates a higher affinity for this disaccharide by allowing two binding modes. PubMed: 14729339DOI: 10.1016/j.jmb.2003.11.043 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.05 Å) |
Structure validation
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