1NPL

MANNOSE-SPECIFIC AGGLUTININ (LECTIN) FROM DAFFODIL (NARCISSUS PSEUDONARCISSUS) BULBS IN COMPLEX WITH MANNOSE-ALPHA1,3-MANNOSE

1NPL の概要

• エントリーDOI: 10.2210/pdb1npl/pdb
• 関連するBIRD辞書のPRD_ID: PRD_900112
• 分子名称: PROTEIN (AGGLUTININ), alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose, PHOSPHATE ION, ... (4 entities in total)
• 機能のキーワード: lectin, agglutinin, mannobiose, mannose-alpha1, 3-mannose, daffodil, sugar binding protein
• 由来する生物種: Narcissus pseudonarcissus (daffodil)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13863.65

構造登録者

Sauerborn, M.K.,Wright, L.M.,Reynolds, C.D.,Grossmann, J.G.,Rizkallah, P.J. (登録日: 1998-12-17, 公開日: 1998-12-23, 最終更新日: 2024-11-20)

主引用文献

Sauerborn, M.K.,Wright, L.M.,Reynolds, C.D.,Grossmann, J.G.,Rizkallah, P.J.
Insights into carbohydrate recognition by Narcissus pseudonarcissus lectin: the crystal structure at 2 A resolution in complex with alpha1-3 mannobiose.
J.Mol.Biol., 290:185-199, 1999

PubMed Abstract: Carbohydrate recognition by monocot mannose-binding lectins was studied via the crystal structure determination of daffodil (Narcissus pseudonarcissus) lectin. The lectin was extracted from daffodil bulbs, and crystallised in the presence of alpha-1,3 mannobiose. Molecular replacement methods were used to solve the structure using the partially refined model of Hippeastrum hybrid agglutinin as a search model. The structure was refined at 2.0 A resolution to a final R -factor of 18.7 %, and Rfreeof 26.7 %. The main feature of the daffodil lectin structure is the presence of three fully occupied binding pockets per monomer, arranged around the faces of a triangular beta-prism motif. The pockets have identical topology, and can bind mono-, di- or oligosaccharides. Strand exchange forms tightly bound dimers, and higher aggregation states are achieved through hydrophobic patches on the surface, completing a tetramer with internal 222-symmetry. There are therefore 12 fully occupied binding pockets per tetrameric cluster. The tetramer persists in solution, as shown with small-angle X-ray solution scattering. Extensive sideways and out-of-plane interactions between tetramers, some mediated via the ligand, make up the bulk of the lattice contacts.A fourth binding site was also observed. This is unique and has not been observed in similar structures. The site is only partially occupied by a ligand molecule due to the much lower binding affinity. A comparison with the Galanthus nivalis agglutinin/mannopentaose complex suggests an involvement of this site in the recognition mechanism for naturally occurring glycans.

PubMed: 10388566
DOI: 10.1006/jmbi.1999.2862

実験手法

X-RAY DIFFRACTION (2 Å)