1msa: Difference between revisions
New page: left|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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[[Image:1msa.gif|left|200px]]<br /><applet load="1msa" size=" | [[Image:1msa.gif|left|200px]]<br /><applet load="1msa" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1msa, resolution 2.29Å" /> | caption="1msa, resolution 2.29Å" /> | ||
'''MANNOSE-SPECIFIC AGGLUTININ (LECTIN) FROM SNOWDROP (GALANTHUS NIVALIS) BULBS COMPLEXED WITH METHYL-ALPHA-D-MANNOSIDE'''<br /> | '''MANNOSE-SPECIFIC AGGLUTININ (LECTIN) FROM SNOWDROP (GALANTHUS NIVALIS) BULBS COMPLEXED WITH METHYL-ALPHA-D-MANNOSIDE'''<br /> | ||
==Overview== | ==Overview== | ||
Tetrameric Galanthus nivalis agglutinin (50,000 M(r)) belongs to a | 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== | ==About this Structure== | ||
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 MMA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 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]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Hester, G.]] | [[Category: Hester, G.]] | ||
[[Category: Wright, C | [[Category: Wright, C S.]] | ||
[[Category: MMA]] | [[Category: MMA]] | ||
[[Category: methyl-alpha-d-mannoside]] | [[Category: methyl-alpha-d-mannoside]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:58:39 2008'' |
Revision as of 14:58, 21 February 2008
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MANNOSE-SPECIFIC AGGLUTININ (LECTIN) FROM SNOWDROP (GALANTHUS NIVALIS) BULBS COMPLEXED WITH METHYL-ALPHA-D-MANNOSIDE
OverviewOverview
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 StructureAbout this Structure
1MSA is a Single protein structure of sequence from Galanthus nivalis with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
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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