1msa: Difference between revisions
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'''MANNOSE-SPECIFIC AGGLUTININ (LECTIN) FROM SNOWDROP (GALANTHUS NIVALIS) BULBS COMPLEXED WITH METHYL-ALPHA-D-MANNOSIDE''' | '''MANNOSE-SPECIFIC AGGLUTININ (LECTIN) FROM SNOWDROP (GALANTHUS NIVALIS) BULBS COMPLEXED WITH METHYL-ALPHA-D-MANNOSIDE''' | ||
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[[Category: Hester, G.]] | [[Category: Hester, G.]] | ||
[[Category: Wright, C S.]] | [[Category: Wright, C S.]] | ||
[[Category: | [[Category: Methyl-alpha-d-mannoside]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:39:48 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 22:39, 2 May 2008
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. 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 Page seeded by OCA on Sat May 3 01:39:48 2008
