Hevein domains protein-carbohydrate interactions

N. Aboitiz, M. Vila-Perello, P. Groves, J. L. Asensio, D. Andreu, F. J. Canada, and J. Jimenez-Barbero, NMR and modeling studies of protein-carbohydrate interactions Synthesis, three-dimensional structure, and recognition properties of a minimum hevein domain with binding affinity for chitooligosaccharides, ChemBioChem, 5 (2004) 1245-1255. 

J. L. Asensio, H.-C. Siebert, C.-W. von der Lieth, J. Laynez, M. Bruix, U. M. S. Soedjanaatmadja, J. J. Beintema, F. J. Canada, H. J. Gabius, and J. Jimenez-Barbero, NMR investigations of protein-carbohydrate interactions Studies on the relevance of Trp/Tyr variations in lectin binding sites as deduced from titration microcalorimetry and NMR studies on hevein domains. Determination of the NMR structure of the complex between pseudo-hevein and YA Y -triacetylchitotriose, Proteins, 40 (2000) 218-236. 

HEVEIN DOMAINS AN ATTRACTIVE MODEL TO STUDY CARBOHYDRATE-PROTEIN INTERACTIONS AT ATOMIC RESOLUTION... 

The small size of hevein (43 residues), and the ease of its availability by biochemical purification or methods of peptide synthesis make this domain an excellent model system for the study of carbohydrate recognition by proteins. Herein, and taking the hevein domain as a model, we focus on the study of those molecular-recognition features relevant for the interactions between carbohydrates and proteins. We detail all of the techniques that are instrumental for tackling this problem, and how these can strategically be combined in an efficient manner. Particular emphasis is placed on the acquisition and analysis of data at atomic resolution (by NMR and/or X-ray ), and how these structural data relate with thermodynamic and kinetic information in reaching an understanding of the forces and interactions that play decisive roles in the interactions between carbohydrates and proteins. 

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