1qmo | pdb_00001qmo

Structure of FRIL, a legume lectin that delays hematopoietic progenitor maturation

spinqualitylabelsall models 1qmo, resolution 3.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1qmo is a 8 chain structure with sequence from Lablab purpureus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.5Å Ligands: CA, MAN, MN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function FRIL_LABPU Mannose-binding lectin (PubMed:9892687). Accommodates most effectively a non-reducing terminal alpha-d-mannosyl unit. Strongly precipitates murine IgM but not IgG (PubMed:9949194). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Binding of multivalent glycoconjugates by lectins often leads to the formation of cross-linked complexes. Type I cross-links, which are one-dimensional, are formed by a divalent lectin and a divalent glycoconjugate. Type II cross-links, which are two or three-dimensional, occur when a lectin or glycoconjugate has a valence greater than two. Type II complexes are a source of additional specificity, since homogeneous type II complexes are formed in the presence of mixtures of lectins and glycoconjugates. This additional specificity is thought to become important when a lectin interacts with clusters of glycoconjugates, e.g. as is present on the cell surface. The cryst1al structure of the Glc/Man binding legume lectin FRIL in complex with a trisaccharide provides a molecular snapshot of how weak protein-protein interactions, which are not observed in solution, can become important when a cross-linked complex is formed. In solution, FRIL is a divalent dimer, but in the crystal FRIL forms a tetramer, which allows for the formation of an intricate type II cross-linked complex with the divalent trisaccharide. The dependence on weak protein-protein interactions can ensure that a specific type II cross-linked complex and its associated specificity can occur only under stringent conditions, which explains why lectins are often found forming higher-order oligomers. The role of weak protein-protein interactions in multivalent lectin-carbohydrate binding: crystal structure of cross-linked FRIL.,Hamelryck TW, Moore JG, Chrispeels MJ, Loris R, Wyns L J Mol Biol. 2000 Jun 16;299(4):875-83. PMID:10843844 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Mannose-binding protein

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