A novel tetrameric lectin from Lycoris aurea with four mannose binding sites per monomer

• Autorzy: Liu J. , Xu X. , Liu J. , Balzarini J. , Luo Y. , Kong Y. , Li J. , Chen F. , Van Damme E. , Bao J.
• Języki publikacji: EN

Abstrakty

EN

The mannose-binding agglutinin from bulbs of Lycoris aurea (LAA) agglutinates rabbit but not human erythrocytes. The molecular mass of the monomer in SDS/PAGE is 12 kDa while the apparent molecular mass in gel filtration is 48 kDa, indicating that LAA is a homotetramer. The full-length cDNA of LAA contains 683 bp with an open reading frame encoding a protomer of 162 amino-acid residues. Hydrophobic Cluster Analysis and molecular modeling of the 109-residue mature polypeptide suggested a similar secondary and tertiary structure to those of Narcissus pseudonarcissus agglutinin (NPA). Molecular docking revealed that, besides the three mannose-binding sites common among Amaryllidaceae lectins, LAA also contains a fourth unique mannose-binding site formed by a tryptophan cluster. The existence of four mannose-binding sites in each monomer of LAA is very unusual and has only been reported for NPA earlier.

Słowa kluczowe

EN

lectin; molecular modelling; Amaryllidaceae; Narcissus pseudonarcissus; mannose binding lectin; fructose; mannose binding agglutinin; Lycoris aurea; agglutinin; bulb; galactose

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2007
• Tom: 54
• Numer: 1
• Opis fizyczny: p.159-166,fig.,ref.

Twórcy

autor

Liu J.

• Sichuan University, Chengdu, 610064, P.R.China

autor

Xu X.

autor

Liu J.

autor

Balzarini J.

autor

Luo Y.

autor

Kong Y.

autor

Li J.

autor

Chen F.

autor

Van Damme E.

autor

Bao J.

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