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1is4

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|RELATEDENTRY=[[1c1l|1C1L]], [[1is3|1IS3]], [[1is5|1IS5]], [[1is6|1IS6]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1is4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1is4 OCA], [http://www.ebi.ac.uk/pdbsum/1is4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1is4 RCSB]</span>
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[[Category: Shirai, T.]]
[[Category: Shirai, T.]]
[[Category: Yamane, T.]]
[[Category: Yamane, T.]]
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[[Category: LAT]]
 
[[Category: beta sandwich]]
[[Category: beta sandwich]]
[[Category: complex with lactose]]
[[Category: complex with lactose]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:54:14 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:23:53 2008''

Revision as of 18:23, 30 March 2008


PDB ID 1is4

Drag the structure with the mouse to rotate
, resolution 1.90Å
Ligands:
Related: 1C1L, 1IS3, 1IS5, 1IS6


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



LACTOSE-LIGANDED CONGERIN II


Overview

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

1IS4 is a Single protein structure of sequence from Conger myriaster. Full crystallographic information is available from OCA.

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:12206768

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