High-resolution crystal structures of Erythrina cristagalli lectin in complex with lactose and 2′-α-L-fucosyllactose and correlation with thermodynamic binding data

Cecilia Svensson, Susann Teneberg, Carol L. Nilsson, Anders Kjellberg, Frederick P. Schwarz, Nathan Sharon, Ute Krengel

Research output: Contribution to journalArticle

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Abstract

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′-α-L-fucosyllactose were determined at 1.6 Å and 1.7 Å 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′-α-L-fucosyllactose, and with two modeled complexes of ECorL with 2′-α-L-fucosyl-N-acetyllactosamine. The molecular models are very similar to the crystal structure of ECL in complex with 2′-α-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.

Original languageEnglish (US)
Pages (from-to)69-83
Number of pages15
JournalJournal of Molecular Biology
Volume321
Issue number1
DOIs
StatePublished - 2002
Externally publishedYes

Fingerprint

Lactose
Thermodynamics
Lectins
Fucose
Binding Sites
Molecular Models
Hydrophobic and Hydrophilic Interactions
Hydrogen
Mass Spectrometry
Theoretical Models
Carbohydrates
erythrina lectin
2'-fucosyllactose
Water

Keywords

  • Crystal structure
  • Glycobiology
  • Lectin
  • Protein-carbohydrate interactions
  • Structure/function

ASJC Scopus subject areas

  • Virology

Cite this

High-resolution crystal structures of Erythrina cristagalli lectin in complex with lactose and 2′-α-L-fucosyllactose and correlation with thermodynamic binding data. / Svensson, Cecilia; Teneberg, Susann; Nilsson, Carol L.; Kjellberg, Anders; Schwarz, Frederick P.; Sharon, Nathan; Krengel, Ute.

In: Journal of Molecular Biology, Vol. 321, No. 1, 2002, p. 69-83.

Research output: Contribution to journalArticle

Svensson, Cecilia ; Teneberg, Susann ; Nilsson, Carol L. ; Kjellberg, Anders ; Schwarz, Frederick P. ; Sharon, Nathan ; Krengel, Ute. / High-resolution crystal structures of Erythrina cristagalli lectin in complex with lactose and 2′-α-L-fucosyllactose and correlation with thermodynamic binding data. In: Journal of Molecular Biology. 2002 ; Vol. 321, No. 1. pp. 69-83.
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abstract = "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′-α-L-fucosyllactose were determined at 1.6 {\AA} and 1.7 {\AA} 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′-α-L-fucosyllactose, and with two modeled complexes of ECorL with 2′-α-L-fucosyl-N-acetyllactosamine. The molecular models are very similar to the crystal structure of ECL in complex with 2′-α-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.",
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AU - Nilsson, Carol L.

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AU - Schwarz, Frederick P.

AU - Sharon, Nathan

AU - Krengel, Ute

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