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Eur J Biochem. 2000 Aug;267(16):5257-64.

The amino-acid sequence of the abalone (Haliotis laevigata) nacre protein perlucin. Detection of a functional C-type lectin domain with galactose/mannose specificity.

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1
Max-Planck-Institut für Biochemie, Martinsried, Germany. mann@biochem.mpg.de

Abstract

Perlucin isolated from abalone nacre consists of 155 amino acids including a glycosylated asparagine. The sequence of the first 130 amino acids shows a high similarity to the C-type carbohydrate-recognition domains of asialoglycoprotein receptors and other members of the group of C-type lectins but also a weaker similarity to related proteins without carbohydrate-binding activity. This C-type module is followed by a short C-terminal domain containing two almost identical sequence repeats with a length of 10 amino acids. Solid phase assays show a divalent metal ion-dependent binding of perlucin to (neo)glycoproteins containing D-galactose or D-mannose/D-glucose indicating that perlucin is a functional C-type lectin with broad carbohydrate-binding specificity. Our results also indicate that it may be difficult to predict carbohydrate-binding specificity and the occurrence of alternative binding configurations by amino-acid sequence comparisons and homology modeling.

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