1is6: Difference between revisions
New page: left|200px<br /><applet load="1is6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1is6, resolution 1.7Å" /> '''MES-Liganded Congerin... |
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[[Image:1is6.jpg|left|200px]]<br /><applet load="1is6" size=" | [[Image:1is6.jpg|left|200px]]<br /><applet load="1is6" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1is6, resolution 1.7Å" /> | caption="1is6, resolution 1.7Å" /> | ||
'''MES-Liganded Congerin II'''<br /> | '''MES-Liganded Congerin II'''<br /> | ||
==Overview== | ==Overview== | ||
The crystal structure of congerin II, a galectin family lectin from conger | The crystal structure of congerin II, a galectin family lectin from conger eel, was determined at 1.45A resolution. The previously determined structure of its isoform, congerin I, had revealed a fold evolution via strand swap; however, the structure of congerin II described here resembles other prototype galectins. A comparison of the two congerin genes with that of several other galectins suggests acceralated evolution of both congerin genes following gene duplication. The presence of a Mes (2-[N-morpholino]ethanesulfonic acid) molecule near the carbohydrate-binding site in the crystal structure points to the possibility of an additional binding site in congerin II. The binding site consists of a group of residues that had been replaced following gene duplication suggesting that the binding site was built under selective pressure. Congerin II may be a protein specialized for biological defense with an affinity for target carbohydrates on parasites' cell surface. | ||
==About this Structure== | ==About this Structure== | ||
1IS6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Conger_myriaster Conger myriaster] with MES as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1IS6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Conger_myriaster Conger myriaster] with <scene name='pdbligand=MES:'>MES</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IS6 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: mes complex]] | [[Category: mes complex]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:15:03 2008'' | ||
Revision as of 14:15, 21 February 2008
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MES-Liganded Congerin II
OverviewOverview
The crystal structure of congerin II, a galectin family lectin from conger eel, was determined at 1.45A resolution. The previously determined structure of its isoform, congerin I, had revealed a fold evolution via strand swap; however, the structure of congerin II described here resembles other prototype galectins. A comparison of the two congerin genes with that of several other galectins suggests acceralated evolution of both congerin genes following gene duplication. The presence of a Mes (2-[N-morpholino]ethanesulfonic acid) molecule near the carbohydrate-binding site in the crystal structure points to the possibility of an additional binding site in congerin II. The binding site consists of a group of residues that had been replaced following gene duplication suggesting that the binding site was built under selective pressure. Congerin II may be a protein specialized for biological defense with an affinity for target carbohydrates on parasites' cell surface.
About this StructureAbout this Structure
1IS6 is a Single protein structure of sequence from Conger myriaster with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of a conger eel galectin (congerin II) at 1.45A resolution: implication for the accelerated evolution of a new ligand-binding site following gene duplication., Shirai T, Matsui Y, Shionyu-Mitsuyama C, Yamane T, Kamiya H, Ishii C, Ogawa T, Muramoto K, J Mol Biol. 2002 Aug 30;321(5):879-89. PMID:12206768
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