Sequence and structural determinants of mannose recognition.
Mannose, an abundant cell surface monosaccharide binds to a diverse set of receptors, which are involved in a variety of important cellular processes. Structural analysis has been carried out on all the proteins containing non-covalently bound mannose as a monosaccharide in the Protein Data Bank, to identify common recognition principles. Proteins, highly specific to mannose, belonging to the super family of bulb lectins, are found to contain a consensus sequence motif QXDXNXVXY, which has been identified to be essential for mannose binding. Analysis of this motif in the crystal structures of bulb lectins has led to the understanding of the contribution of individual residues in mannose recognition. Comparison with other mannose binding proteins, reveals common hydrogen bonding patterns in all of them, despite differences in sequence, overall fold and the substructures at the binding sites of individual proteins. A database analysis also suggests that although the topology of the backbone, as at the binding site in bulb lectins, can generate mannose binding capability in a few other proteins, sequence and disposition of not only the residues in the motif, but also the residues in the neighborhood play a crucial role in allowing that property to be retained.
Ramachandraiah
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G
Molecular Biophysics Unit, Bangalore, India.
Chandra
N R
NR
D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D000818:Animals; D037102:Lectins / Q000737:chemistry* / Q000378:metabolism; D008358:Mannose / Q000378:metabolism*; D008969:Molecular Sequence Data; D011506:Proteins / Q000378:metabolism
D037102:Lectins; D011506:Proteins; D008358:Mannose