1msa

Publication Abstract from PubMed

Tetrameric Galanthus nivalis agglutinin (50,000 M(r)) belongs to a super-family of alpha-D-mannose-specific plant bulb lectins known to be potent inhibitors of retroviruses. The 2.3 A crystal structure of this lectin complexed with methyl alpha-D-mannose reveals a novel three-fold symmetric beta-sheet polypeptide fold. Three antiparallel four-stranded beta-sheets, each with a conserved mannose-binding site, are arranged as a 12-stranded beta-barrel. The tetramer displays 222 symmetry. Pairs of monomers form stable dimers through C-terminal strand exchange. The so formed hybrid beta-sheets are the sites for high affinity mannose binding in the dimer interface. Occupancy observed at corresponding sites in other beta-sheets suggests a potential for twelve sites per tetramer.

Structure of mannose-specific snowdrop (Galanthus nivalis) lectin is representative of a new plant lectin family.,Hester G, Kaku H, Goldstein IJ, Wright CS Nat Struct Biol. 1995 Jun;2(6):472-9. PMID:7664110^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.