1G5N

ANNEXIN V COMPLEX WITH HEPARIN OLIGOSACCHARIDES

Summary for 1G5N

• Entry DOI: 10.2210/pdb1g5n/pdb
• Descriptor: ANNEXIN V, 4-deoxy-2-O-sulfo-alpha-L-threo-hex-4-enopyranuronic acid-(1-4)-2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose-(1-4)-2-O-sulfo-alpha-L-idopyranuronic acid-(1-4)-2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: helix-bundle, membrane binding, heparin, heparan sulfate, blood clotting
• Biological source: Rattus norvegicus (Norway rat)
• Total number of polymer chains: 1
• Total formula weight: 38327.85

Authors

Capila, I.,Heraiz, M.J.,Mo, Y.D.,Mealy, T.R.,Campos, B.,Dedman, J.R.,Linhardt, R.J.,Seaton, B.A. (deposition date: 2000-11-01, release date: 2001-06-06, Last modification date: 2024-04-03)

Primary citation

Capila, I.,Hernaiz, M.J.,Mo, Y.D.,Mealy, T.R.,Campos, B.,Dedman, J.R.,Linhardt, R.J.,Seaton, B.A.
Annexin V--heparin oligosaccharide complex suggests heparan sulfate--mediated assembly on cell surfaces.
Structure, 9:57-64, 2001

PubMed Abstract: Annexin V, an abundant anticoagulant protein, has been proposed to exert its effects by self-assembling into highly ordered arrays on phospholipid membranes to form a protective anti-thrombotic shield at the cell surface. The protein exhibits very high-affinity calcium-dependent interactions with acidic phospholipid membranes, as well as specific binding to glycosaminoglycans (GAGs) such as heparin and heparan sulfate, a major component of cell surface proteoglycans. At present, there is no structural information to elucidate this interaction or the role it may play in annexin V function at the cell surface.

PubMed: 11342135
DOI: 10.1016/S0969-2126(00)00549-9

Experimental method

X-RAY DIFFRACTION (1.9 Å)