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1lul

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[[Image:1lul.jpg|left|200px]]
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{{Seed}}
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[[Image:1lul.png|left|200px]]
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{{STRUCTURE_1lul| PDB=1lul | SCENE= }}
{{STRUCTURE_1lul| PDB=1lul | SCENE= }}
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'''DB58, A LEGUME LECTIN FROM DOLICHOS BIFLORUS'''
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===DB58, A LEGUME LECTIN FROM DOLICHOS BIFLORUS===
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==Overview==
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The seed lectin (DBL) from the leguminous plant Dolichos biflorus has a unique specificity among the members of the legume lectin family because of its high preference for GalNAc over Gal. In addition, precipitation of blood group A+H substance by DBL is slightly better inhibited by a blood group A trisaccharide (GalNAc(alpha1-3)[Fuc(alpha1-2)]Gal) containing pentasaccharide, and about 40 times better by the Forssman disaccharide (GalNAc(alpha1-3)GalNAc) than by GalNAc. We report the crystal structures of the DBL-blood group A trisaccharide complex and the DBL-Forssman disaccharide complex.A comparison with the binding sites of Gal-binding legume lectins indicates that the low affinity of DBL for Gal is due to the substitution of a conserved aromatic residue by an aliphatic residue (Leu127). Binding studies with a Leu127Phe mutant corroborate these conclusions. DBL has a higher affinity for GalNAc because the N-acetyl group compensates for the loss of aromatic stacking in DBL by making a hydrogen bond with the backbone amide group of Gly103 and a hydrophobic contact with the side-chains of Trp132 and Tyr104.Some legume lectins possess a hydrophobic binding site that binds adenine and adenine-derived plant hormones, i.e. cytokinins. The exact function of this binding site is unknown, but adenine/cytokinin-binding legume lectins might be involved in storage of plant hormones or plant growth regulation. The structures of DBL in complex with adenine and of the dimeric stem and leaf lectin (DB58) from the same plant provide the first structural data on these binding sites. Both oligomers possess an unusual architecture, featuring an alpha-helix sandwiched between two monomers. In both oligomers, this alpha-helix is directly involved in the formation of the hydrophobic binding site. DB58 adopts a novel quaternary structure, related to the quaternary structure of the DBL heterotetramer, and brings the number of know legume lectin dimer types to four.
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(as it appears on PubMed at http://www.pubmed.gov), where 10047489 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10047489}}
==About this Structure==
==About this Structure==
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[[Category: Plant hormone binding]]
[[Category: Plant hormone binding]]
[[Category: Quaternary structure]]
[[Category: Quaternary structure]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:18:20 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 22:19:10 2008''

Revision as of 19:19, 2 July 2008

Image:1lul.png

Template:STRUCTURE 1lul

DB58, A LEGUME LECTIN FROM DOLICHOS BIFLORUS

Template:ABSTRACT PUBMED 10047489

About this Structure

1LUL is a Single protein structure of sequence from Vigna unguiculata subsp. cylindrica. Full crystallographic information is available from OCA.

Reference

Carbohydrate binding, quaternary structure and a novel hydrophobic binding site in two legume lectin oligomers from Dolichos biflorus., Hamelryck TW, Loris R, Bouckaert J, Dao-Thi MH, Strecker G, Imberty A, Fernandez E, Wyns L, Etzler ME, J Mol Biol. 1999 Mar 5;286(4):1161-77. PMID:10047489

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