Animal lectins

S-type lectins P-Galactoside-binding animal lectins with roles In cell-cell and cell-matrix interactions... 

K. N. Konstantinov, B. A. Robbins, and F.-T. Liu, Galectin-3, a /l-galactoside-binding animal lectin, is a marker of anaplastic large-cell lymphoma, Am. J. Path., 148 (1996) 25-30. 

A number of carbohydrate recognition domains (CRDs) of animal lectins are known to exist as clusters. ASGP-Rs exist as bundle of hexamers, mannose 6-phosphate receptor and galectin-3 are known as dimers, while mannose binding proteins and receptors form multiple CRDs [31]. 

Kilpatrick, D.C. (2002) Animal lectins a historical introduction and overview. Biochim. Biophys. Acta 1572, 187-197. 

K. Drickamer, Two distinct classes of carbohydrate-recognition domains in animal lectins, J. Biol. Chem. 263 9557 (1988). 

H. Egge The use of FAB-MS for the study of oligosaccharides Y. C. Lee Topography of binding site of animal lectins... 

Drickamer K (1994) Molecular structure of animal lectins. In Fukuda M, Hindsgaul O (eds) Frontiers in Molecular Biology, Molecular Glycobiology. IRL Press, Oxford, p 53... 

Although the physiological function of plant and animal lectins is unknown, these ubiquitous carbohydrate-binding (glyco)proteins can recognize and bind to complex carbohydrates as they occur in solution and on membranes and cell surfaces. A series of papers (by Hardman Brewer and Brown Williams and coworkers Thomas and colleagues and Evans and Wang) deal with the fundamental chemistry of lectin... 

D. C. Kilpatrick, Handbook of Animal Lectins Properties and Biomedical Applications, Wiley, Chichester, 2000. 

E. R. Gold and P. Balding, Receptor-Specific Proteins, Plant and Animal Lectins, American Elsevier, New York, 1975, pp. 1-440. 

Links to crystal stmctures of lectins in PDB organized based on algal, fungal, bacterial, viral, plant, and animal lectins. 

The groups of Monsigny and colleagues (7, 8) and Iyer and Goldstein (9) prepared neoglycoproteins for specificity studies of plant lectins (7, 8). The specificity studies later were extended to animal lectins (4, 68-70) with excellent results. 

Figure 11.29. Structure of a C-Type Carbohydrate-Bindiug Domain from an Animal Lectin. A calcium ion links a mannose residue to the lectin. Selected interactions are shown, with some hydrogen atoms omitted for clarity.

Selected families ef animal lectins classified according to known sequence homologies [12,102,105]... 

Gabius H-J (ed) (2002) Animal Lectins, Biochim Biophys Acta 1572 163... 

The interesting chemistry of sialic acid has been discussed in several reviews [213,214,215]. Sialic acid is an important component of complex oligosaccharides, when it is placed in the terminal position, and often masks the penultimate saccharide sequences. In this position, it interacts with numerous receptors including the influenza virus neuraminidase, and receptors mediating intercellular interactions such as the selectins (members of the C-t) e animal lectin family) and siglecs (or sialoadhesins, members of the immunoglobulin superfamily). The structure of influenza B neuraminidase in complex with sialic acid has been solved by X-ray crystallography at 2.2 A resolution (O Fig. 17) [216]. 

Structure of a C-type carbohydrale-binding domain from an animal lectin Figure 11.26... 

Gold, A.P. and Balding, P. (1975) Receptor-specific proteins, plant and animal lectins. 

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