The covalent and three-dimensional structural of concanavalin A. I. Amino acid sequence of cyanogen bromide fragments F1 and F2.

Concanavalin A is a lectin composed of identical subunits, each containg 237 amino acid residues. The complete amino acid sequence of the first 129 residues of the polypeptide chain has been determined by analysis of peptides obtained from digests of CNBr Fragments F1 (residues 1 to 42) and F2 (residues 40 to 129). Correlation of the chemical sequence with x-ray crystallographic results indicates that Fragment F1 contains all of the protein ligands for the binding of 2 metal ions, Mn2+ and Ca2+, and that Fragment F2 contains many of the residues involved in the interactions of the subunits to form dimers and tetramers. The site of cleavage of the polypeptide chain to yield the naturally occurring Fragments A1 and A2 has also been identified as the peptide bond between residues 118 and 119.

• Publication year

  1975

• Venue

  Journal of Biological Chemistry

• Publication date

  Unknown publication date

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1016/s0021-9258(19)41840-1PMID 1112813
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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