Literature DB >> 12144516

The importance of CH/pi interactions to the function of carbohydrate binding proteins.

Michiro Muraki1.   

Abstract

It is suggested that the interactions between the hydrophobic C-H groups of carbohydrate residues and the pi-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/pi interactions are involved in the actual binding events.

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Year:  2002        PMID： 12144516     DOI： 10.2174/0929866023408751

Source DB:  PubMed          Journal:  Protein Pept Lett        ISSN： 0929-8665            Impact factor:   1.890


  15 in total

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4.  Identification of amino acids important for binding of Clostridium perfringens epsilon toxin to host cells and to HAVCR1.

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5.  Disaccharide binding to galectin-1: free energy calculations and molecular recognition mechanism.

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8.  Exploring the free-energy landscape of carbohydrate-protein complexes: development and validation of scoring functions considering the binding-site topology.

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9.  Analysis of structural water and CH···π interactions in HIV-1 protease and PTP1B complexes using a hydrogen bond prediction tool, HBPredicT.

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