- Tytuł:
- A novel tetrameric lectin from Lycoris aurea with four mannose binding sites per monomer
- Autorzy:
-
Liu, Jiwei
Xu, Xiaochao
Liu, Jinzhi
Balzarini, Jan
Luo, Yongtin
Kong, Yang
Li, Jian
Chen, Fang
Van Damme, Els
Bao, Jinku - Powiązania:
- https://bibliotekanauki.pl/articles/1041131.pdf
- Data publikacji:
- 2007
- Wydawca:
- Polskie Towarzystwo Biochemiczne
- Tematy:
-
sequence alignment
mannose-binding lectin
Lycoris aurea agglutinin
molecular modeling and docking - Opis:
- 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.
- Źródło:
-
Acta Biochimica Polonica; 2007, 54, 1; 159-166
0001-527X - Pojawia się w:
- Acta Biochimica Polonica
- Dostawca treści:
- Biblioteka Nauki
Artykuł