1JPC

MANNOSE-SPECIFIC AGGLUTININ (LECTIN) FROM SNOWDROP (GALANTHUS NIVALIS) BULBS IN COMPLEX WITH MANNOSE-ALPHA1,6-(MANNOSE-ALPHA1,3)-MANNOSE-ALPHA1,6-(MANNOSE-ALPHA1,3)-MANNOSE

1JPC の概要

• エントリーDOI: 10.2210/pdb1jpc/pdb
• 関連するBIRD辞書のPRD_ID: PRD_900118
• 分子名称: AGGLUTININ, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose, alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose, ... (4 entities in total)
• 機能のキーワード: lectin, agglutinin, mannopentaose, (mannose-alpha1, 6-(mannose-alpha1, 3-mannose- alpha1, 3)-mannose), snowdrop
• 由来する生物種: Galanthus nivalis (common snowdrop)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13412.52

構造登録者

Wright, C.S.,Hester, G. (登録日: 1996-07-30, 公開日: 1997-01-27, 最終更新日: 2024-10-16)

主引用文献

Wright, C.S.,Hester, G.
The 2.0 A structure of a cross-linked complex between snowdrop lectin and a branched mannopentaose: evidence for two unique binding modes.
Structure, 4:1339-1352, 1996

PubMed Abstract: Galanthus nivalis agglutinin (GNA), a mannose-specific lectin from snowdrop bulbs, is a tetrameric member of the family of Amaryllidaceae lectins that exhibit antiviral activity towards HIV. Its subunits are composed of three pseudo-symmetrically related beta sheet domains, each with a conserved mannose-binding site. Crystal structures of monosaccharide and disaccharide complexes of GNA have revealed that all 12 binding sites of the tetramer are functional, and that the degree of occupancy is dependent on the availability of subsidiary interactions from neighboring subunits. The complex of GNA with a branched mannopentaose ((Manalpha1,6-(alpha1, 3-Man)Man-alpha1,6-(alpha1,3-Man)Man) described here simulates a more biologically relevant complex.

PubMed: 8939757
DOI: 10.1016/S0969-2126(96)00141-4

実験手法

X-RAY DIFFRACTION (2 Å)