1msa
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(New page: 200px<br /><applet load="1msa" size="450" color="white" frame="true" align="right" spinBox="true" caption="1msa, resolution 2.29Å" /> '''MANNOSE-SPECIFIC AGG...)
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Revision as of 19:32, 20 November 2007
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MANNOSE-SPECIFIC AGGLUTININ (LECTIN) FROM SNOWDROP (GALANTHUS NIVALIS) BULBS COMPLEXED WITH METHYL-ALPHA-D-MANNOSIDE
Overview
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.
About this Structure
1MSA is a Single protein structure of sequence from Galanthus nivalis with MMA as ligand. Full crystallographic information is available from OCA.
Reference
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
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