1ciw
From Proteopedia
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|PDB= 1ciw |SIZE=350|CAPTION= <scene name='initialview01'>1ciw</scene>, resolution 2.70Å | |PDB= 1ciw |SIZE=350|CAPTION= <scene name='initialview01'>1ciw</scene>, resolution 2.70Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ciw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ciw OCA], [http://www.ebi.ac.uk/pdbsum/1ciw PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ciw RCSB]</span> | ||
}} | }} | ||
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[[Category: Surolia, A.]] | [[Category: Surolia, A.]] | ||
[[Category: Vijayan, M.]] | [[Category: Vijayan, M.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: MN]] | ||
[[Category: agglutinin]] | [[Category: agglutinin]] | ||
[[Category: carbohydrate specificity]] | [[Category: carbohydrate specificity]] | ||
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[[Category: water bridge]] | [[Category: water bridge]] | ||
| - | ''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 19:22:41 2008'' |
Revision as of 16:22, 30 March 2008
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| , resolution 2.70Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
PEANUT LECTIN COMPLEXED WITH N-ACETYLLACTOSAMINE
Overview
The crystal structures of complexes of peanut lectin with methyl-beta-galactose and N-acetyllactosamine have been determined at 2.8 and 2.7 A, respectively. These, and the complexes involving lactose and the T-antigenic disaccharide reported previously, permit a detailed characterization of peanut-lectin-carbohydrate association and the role of water molecules therein. The water molecules in the combining site are substantially conserved in the four complexes. The role of interacting sugar hydroxyl groups, when absent, are often mimicked by ordered water molecules not only at the primary combining site, but also at the site of the second sugar ring. The similarity of peanut-lectin-sugar interactions with those in other galactose/N-acetylgalactosamine-specific lectins also extend to a substantial degree to water bridges. The comparative study provides a structural explanation for the exclusive specificity of peanut lectin for galactose at the monosaccharide level, compared with that of the other lectins for galactose as well as N-acetylgalactosamine. The complexes also provide a qualitative structural rationale for differences in the strengths of binding of peanut lectin to different sugars.
About this Structure
1CIW is a Single protein structure of sequence from Arachis hypogaea. Full crystallographic information is available from OCA.
Reference
Structures of the complexes of peanut lectin with methyl-beta-galactose and N-acetyllactosamine and a comparative study of carbohydrate binding in Gal/GalNAc-specific legume lectins., Ravishankar R, Suguna K, Surolia A, Vijayan M, Acta Crystallogr D Biol Crystallogr. 1999 Aug;55(Pt 8):1375-82. PMID:10417405
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