1lte

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(New page: 200px<br /><applet load="1lte" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lte, resolution 2.0&Aring;" /> '''STRUCTURE OF A LEGUME...)
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[[Image:1lte.gif|left|200px]]<br /><applet load="1lte" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1lte, resolution 2.0&Aring;" />
caption="1lte, resolution 2.0&Aring;" />
'''STRUCTURE OF A LEGUME LECTIN WITH AN ORDERED N-LINKED CARBOHYDRATE IN COMPLEX WITH LACTOSE'''<br />
'''STRUCTURE OF A LEGUME LECTIN WITH AN ORDERED N-LINKED CARBOHYDRATE IN COMPLEX WITH LACTOSE'''<br />
==Overview==
==Overview==
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The three-dimensional structure of the lactose complex of the Erythrina, corallodendron lectin (EcorL), a dimer of N-glycosylated subunits, was, determined crystallographically and refined at 2.0 angstrom resolution to, an R value of 0.19. The tertiary structure of the subunit is similar to, that of other legume lectins, but interference by the bulky N-linked, heptasaccharide, which is exceptionally well ordered in the crystal, forces the EcorL dimer into a drastically different quaternary structure., Only the galactose moiety of the lactose ligand resides within the, combining site. The galactose moiety is oriented differently from ligands, in the mannose-glucose specific legume lectins and is held by hydrophobic, interactions with Ala88, Tyr106, Phe131, and Ala218 and by seven hydrogen, bonds, four of which are to the conserved Asp89, Asn133, and NH of Gly107., The specificity of legume lectins toward the different C-4 epimers appears, to be associated with extensive variations in the outline of the variable, parts of the binding sites.
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The three-dimensional structure of the lactose complex of the Erythrina corallodendron lectin (EcorL), a dimer of N-glycosylated subunits, was determined crystallographically and refined at 2.0 angstrom resolution to an R value of 0.19. The tertiary structure of the subunit is similar to that of other legume lectins, but interference by the bulky N-linked heptasaccharide, which is exceptionally well ordered in the crystal, forces the EcorL dimer into a drastically different quaternary structure. Only the galactose moiety of the lactose ligand resides within the combining site. The galactose moiety is oriented differently from ligands in the mannose-glucose specific legume lectins and is held by hydrophobic interactions with Ala88, Tyr106, Phe131, and Ala218 and by seven hydrogen bonds, four of which are to the conserved Asp89, Asn133, and NH of Gly107. The specificity of legume lectins toward the different C-4 epimers appears to be associated with extensive variations in the outline of the variable parts of the binding sites.
==About this Structure==
==About this Structure==
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1LTE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with MN and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LTE OCA].
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1LTE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=MN:'>MN</scene> and <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LTE OCA].
==Reference==
==Reference==
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[[Category: lectin]]
[[Category: lectin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:51:58 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:48:21 2008''

Revision as of 11:48, 21 February 2008


1lte, resolution 2.0Å

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STRUCTURE OF A LEGUME LECTIN WITH AN ORDERED N-LINKED CARBOHYDRATE IN COMPLEX WITH LACTOSE

Overview

The three-dimensional structure of the lactose complex of the Erythrina corallodendron lectin (EcorL), a dimer of N-glycosylated subunits, was determined crystallographically and refined at 2.0 angstrom resolution to an R value of 0.19. The tertiary structure of the subunit is similar to that of other legume lectins, but interference by the bulky N-linked heptasaccharide, which is exceptionally well ordered in the crystal, forces the EcorL dimer into a drastically different quaternary structure. Only the galactose moiety of the lactose ligand resides within the combining site. The galactose moiety is oriented differently from ligands in the mannose-glucose specific legume lectins and is held by hydrophobic interactions with Ala88, Tyr106, Phe131, and Ala218 and by seven hydrogen bonds, four of which are to the conserved Asp89, Asn133, and NH of Gly107. The specificity of legume lectins toward the different C-4 epimers appears to be associated with extensive variations in the outline of the variable parts of the binding sites.

About this Structure

1LTE is a Single protein structure of sequence from [1] with and as ligands. Full crystallographic information is available from OCA.

Reference

Structure of a legume lectin with an ordered N-linked carbohydrate in complex with lactose., Shaanan B, Lis H, Sharon N, Science. 1991 Nov 8;254(5033):862-6. PMID:1948067

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