1gz9
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The primary sequence of Erythrina cristagalli lectin (ECL) was mapped by, mass spectrometry, and the crystal structures of the lectin in complex, with lactose and 2'-alpha-L-fucosyllactose were determined at 1.6A and, 1.7A resolution, respectively. The two complexes were compared with the, crystal structure of the closely related Erythrina corallodendron lectin, (ECorL) in complex with lactose, with the crystal structure of the Ulex, europaeus lectin II in complex with 2'-alpha-L-fucosyllactose, and with, two modeled complexes of ECorL with, 2'-alpha-L-fucosyl-N-acetyllactosamine. The molecular models are very, similar to the crystal structure of ECL in complex with, 2'-alpha-L-fucosyllactose with respect to the overall mode of binding, with the L-fucose fitting snugly into the cavity ... | + | The primary sequence of Erythrina cristagalli lectin (ECL) was mapped by, mass spectrometry, and the crystal structures of the lectin in complex, with lactose and 2'-alpha-L-fucosyllactose were determined at 1.6A and, 1.7A resolution, respectively. The two complexes were compared with the, crystal structure of the closely related Erythrina corallodendron lectin, (ECorL) in complex with lactose, with the crystal structure of the Ulex, europaeus lectin II in complex with 2'-alpha-L-fucosyllactose, and with, two modeled complexes of ECorL with, 2'-alpha-L-fucosyl-N-acetyllactosamine. The molecular models are very, similar to the crystal structure of ECL in complex with, 2'-alpha-L-fucosyllactose with respect to the overall mode of binding, with the L-fucose fitting snugly into the cavity surrounded by Tyr106, Tyr108, Trp135 and Pro134 adjoining the primary combining site of the, lectin. Marked differences were however noted between the models and the, experimental structure in the network of hydrogen bonds and hydrophobic, interactions holding the L-fucose in the combining site of the lectin, pointing to limitations of the modeling approach. In addition to the, structural characterization of the ECL complexes, an effort was undertaken, to correlate the structural data with thermodynamic data obtained from, microcalorimetry, revealing the importance of the water network in the, lectin combining site for carbohydrate binding. |
==About this Structure== | ==About this Structure== | ||
| - | 1GZ9 is a | + | 1GZ9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Eukaryota Eukaryota] with MN and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: MNA. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GZ9 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: saccharide]] | [[Category: saccharide]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 12:52:34 2007'' |
Revision as of 10:47, 5 November 2007
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HIGH-RESOLUTION CRYSTAL STRUCTURE OF ERYTHRINA CRISTAGALLI LECTIN IN COMPLEX WITH 2'-ALPHA-L-FUCOSYLLACTOSE
Overview
The primary sequence of Erythrina cristagalli lectin (ECL) was mapped by, mass spectrometry, and the crystal structures of the lectin in complex, with lactose and 2'-alpha-L-fucosyllactose were determined at 1.6A and, 1.7A resolution, respectively. The two complexes were compared with the, crystal structure of the closely related Erythrina corallodendron lectin, (ECorL) in complex with lactose, with the crystal structure of the Ulex, europaeus lectin II in complex with 2'-alpha-L-fucosyllactose, and with, two modeled complexes of ECorL with, 2'-alpha-L-fucosyl-N-acetyllactosamine. The molecular models are very, similar to the crystal structure of ECL in complex with, 2'-alpha-L-fucosyllactose with respect to the overall mode of binding, with the L-fucose fitting snugly into the cavity surrounded by Tyr106, Tyr108, Trp135 and Pro134 adjoining the primary combining site of the, lectin. Marked differences were however noted between the models and the, experimental structure in the network of hydrogen bonds and hydrophobic, interactions holding the L-fucose in the combining site of the lectin, pointing to limitations of the modeling approach. In addition to the, structural characterization of the ECL complexes, an effort was undertaken, to correlate the structural data with thermodynamic data obtained from, microcalorimetry, revealing the importance of the water network in the, lectin combining site for carbohydrate binding.
About this Structure
1GZ9 is a Single protein structure of sequence from Eukaryota with MN and CA as ligands. Structure known Active Site: MNA. Full crystallographic information is available from OCA.
Reference
High-resolution crystal structures of Erythrina cristagalli lectin in complex with lactose and 2'-alpha-L-fucosyllactose and correlation with thermodynamic binding data., Svensson C, Teneberg S, Nilsson CL, Kjellberg A, Schwarz FP, Sharon N, Krengel U, J Mol Biol. 2002 Aug 2;321(1):69-83. PMID:12139934
Page seeded by OCA on Mon Nov 5 12:52:34 2007
Categories: Eukaryota | Single protein | Kjellberg, A. | Krengel, U. | Nilsson, C.L. | Schwarz, F.P. | Sharon, N. | Svensson, C. | Teneberg, S. | CA | MN | Carbohydrate | Crystal structure | Fucose | Fucosyllactose protein-carbohydrate interactions | Glycobiology | Glycoprotein | Lactose | Legume lectin | Protein | Saccharide
