1is6: Difference between revisions
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|PDB= 1is6 |SIZE=350|CAPTION= <scene name='initialview01'>1is6</scene>, resolution 1.7Å | |PDB= 1is6 |SIZE=350|CAPTION= <scene name='initialview01'>1is6</scene>, resolution 1.7Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC ACID'>MES</scene> | |LIGAND= <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1c1l|1C1L]], [[1is3|1IS3]], [[1is4|1IS4]], [[1is5|1IS5]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1is6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1is6 OCA], [http://www.ebi.ac.uk/pdbsum/1is6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1is6 RCSB]</span> | |||
}} | }} | ||
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[[Category: Shirai, T.]] | [[Category: Shirai, T.]] | ||
[[Category: Yamane, T.]] | [[Category: Yamane, T.]] | ||
[[Category: beta sandwich]] | [[Category: beta sandwich]] | ||
[[Category: mes complex]] | [[Category: mes complex]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:23:56 2008'' | ||
Revision as of 21:23, 30 March 2008
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| , resolution 1.7Å | |||||||
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| Ligands: | |||||||
| Related: | 1C1L, 1IS3, 1IS4, 1IS5
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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