1msa: Difference between revisions

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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="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1msa.gif|left|200px]]<br /><applet load="1msa" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1msa, resolution 2.29&Aring;" />
caption="1msa, resolution 2.29&Aring;" />
'''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, 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.
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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MSA OCA].  
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.S.]]
[[Category: Wright, C S.]]
[[Category: MMA]]
[[Category: MMA]]
[[Category: methyl-alpha-d-mannoside]]
[[Category: methyl-alpha-d-mannoside]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:39:52 2007''
''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

File:1msa.gif


1msa, resolution 2.29Å

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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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