1is3: Difference between revisions
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'''LACTOSE AND MES-LIGANDED CONGERIN II''' | {{Structure | ||
|PDB= 1is3 |SIZE=350|CAPTION= <scene name='initialview01'>1is3</scene>, resolution 1.45Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=LAT:LACTOSE'>LAT</scene> and <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC ACID'>MES</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''LACTOSE AND MES-LIGANDED CONGERIN II''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1IS3 is a [ | 1IS3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Conger_myriaster Conger myriaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IS3 OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12206768 12206768] | ||
[[Category: Conger myriaster]] | [[Category: Conger myriaster]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: LAT]] | [[Category: LAT]] | ||
[[Category: MES]] | [[Category: MES]] | ||
[[Category: complex with lactose and | [[Category: complex with lactose and me]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:54:11 2008'' | ||
Revision as of 12:54, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
LACTOSE AND 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
1IS3 is a Single protein structure of sequence from Conger myriaster. 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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