1BUN

STRUCTURE OF BETA2-BUNGAROTOXIN: POTASSIUM CHANNEL BINDING BY KUNITZ MODULES AND TARGETED PHOSPHOLIPASE ACTION

Summary for 1BUN

• Entry DOI: 10.2210/pdb1bun/pdb
• Descriptor: BETA2-BUNGAROTOXIN, SODIUM ION, ... (4 entities in total)
• Functional Keywords: hydrolase, presynaptic neurotoxin, toxin
• Biological source: Bungarus multicinctus (many-banded krait); More
• Cellular location: Secreted: P00617 P00989
• Total number of polymer chains: 2
• Total formula weight: 20780.66

Authors

Kwong, P.D.,Mcdonald, N.Q.,Sigler, P.B.,Hendrickson, W.A. (deposition date: 1995-10-15, release date: 1996-04-03, Last modification date: 2024-10-30)

Primary citation

Kwong, P.D.,McDonald, N.Q.,Sigler, P.B.,Hendrickson, W.A.
Structure of beta 2-bungarotoxin: potassium channel binding by Kunitz modules and targeted phospholipase action.
Structure, 3:1109-1119, 1995

PubMed Abstract: beta-bungarotoxin is a heterodimeric neurotoxin consisting of a phospholipase subunit linked by a disulfide bond to a K+ channel binding subunit which is a member of the Kunitz protease inhibitor superfamily. Toxicity, characterized by blockage of neural transmission, is achieved by the lipolytic action of the phospholipase targeted to the presynaptic membrane by the Kunitz module.

PubMed: 8590005
DOI: 10.1016/S0969-2126(01)00246-5

Experimental method

X-RAY DIFFRACTION (2.45 Å)