Three dimensional structure of erabutoxin b neurotoxic protein: inhibitor of acetylcholine receptor.


Journal Article

The three-dimensional structure of erabutoxin b, a neurotoxin in the venom of the sea snake Laticauda semifasciata, has been determined from a 2.75 A resolution electron density map. Erabutoxin b is one of a family of snake venom neurotoxins, all low-molecular-weight proteins, which block neuromuscular transmission at the postsynaptic membrane. They specifically inhibit the acetylcholine receptor. The molecular shape is that of a shallow elongated saucer with a footed stand formed by the six-membered ring at the COOH-terminal end. The central core of the molecule is an assembly of four disulfide bridges. Three long chain loops emerge as broad fronds from the core region. Approximately 40% of the main chain is organized into a twisted antiparallel beta-pleated sheet of five short strands. In 28 snake venom neurotoxins of established sequence which inhibit the acetylcholine receptor, the four disulfide bridges and seven other residues remain invariant. Three substitution positions conserve residue type. In one wing of the molecule, there is a broad shallow depression which may characterize the reactive site. It is populated by the sevent invariant residues and two of the three type conserved residues. This region is "anchored" on the undersurface of the molecule by the hydroxyl group of Ser-9, the remaining conservatively substituted residue.

Full Text

Duke Authors

Cited Authors

  • Low, BW; Preston, HS; Sato, A; Rosen, LS; Searl, JE; Rudko, AD; Richardson, JS

Published Date

  • September 1, 1976

Published In

Volume / Issue

  • 73 / 9

Start / End Page

  • 2991 - 2994

PubMed ID

  • 1067597

Pubmed Central ID

  • 1067597

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.73.9.2991


  • eng

Conference Location

  • United States