The Importance of Ch / Interactions to the Function of Carbohydrate Binding Proteins

Author: Muraki M.

Source: Protein and Peptide Letters, Volume 9, Number 3, June 2002 , pp. 195-209(15)

Publisher: Bentham Science Publishers

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Abstract:

It is suggested that the interactions between the hydrophobic C-H groups of carbohydrate residues and the p-electron systems of aromatic amino-acid residues play an important role in the ligand-recognition function of carbohydrate-binding proteins. This review focuses on our recent structural and functional studies of human lysozyme and hevein-domain type lectins (wheat-germ agglutinin and Ac-AMP2) aimed at understanding how CH / pgr interactions are involved in the actual binding events.

Keywords: interaction; carbohydrate binding protein; cbp interaction

Language: English

Document Type: Review article

DOI: http://dx.doi.org/10.2174/0929866023408751

Publication date: 2002-06-01

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Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.