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

Summary for 1JPC

• Entry DOI: 10.2210/pdb1jpc/pdb
• Related PRD ID: PRD_900118
• Descriptor: 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)
• Functional Keywords: lectin, agglutinin, mannopentaose, (mannose-alpha1, 6-(mannose-alpha1, 3-mannose- alpha1, 3)-mannose), snowdrop
• Biological source: Galanthus nivalis (common snowdrop)
• Total number of polymer chains: 1
• Total formula weight: 13412.52

Authors

Wright, C.S.,Hester, G. (deposition date: 1996-07-30, release date: 1997-01-27, Last modification date: 2024-10-16)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2 Å)