1msa: Difference between revisions

[[Image:1msa.gif|left|200px]]<br /><applet load="1msa" size="350" color="white" frame="true" align="right" spinBox="true"  

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.

1MSA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Galanthus_nivalis Galanthus nivalis] with <scene name='pdbligand=MMA:'>MMA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MSA OCA].  

[[Category: Wright, C S.]]

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