Lectin structure

J. M. Rini, Lectin structure, Anna. Rev. Biophys. Biomol. Struct., 24 (1995) 551-577. 

R. Loris, T. Hamelryck, J. Bouckaert, and L. Wyns, Legume lectin structure, Biochim. Biophys. Acta, 1383 (1998) 9-36. 

Bourne, Y., Zamboni, V., Barre, A., Peumans, W.J., Van Damme, E.J., and Rouge, P, Helianthus tuberosus lectin reveals a widespread scaffold for mannose-binding lectins, Structure (London), 7, 1473-1482, 1999. 

Calcium one is considered to be involved in maintaining lectin structure while calcium two coordinates directly with carbohydrate, and calcium three is believed to be an artifact of crystallization [20]. 

Turner MW, Hamvas RM. Mannose-binding lectin structure, function, genetics and disease associations. Science 2001 29 2370-6. 

Gabius HJ, Andre S, Jimenez-Barbero J et al (2011) From lectin structure to functional glycomics principles of the sugar code. Trends Biochem Sci 36 288-303... 

Rini JM (1995) Lectin structure. Aimu Rev Biophys Biomol Struct 24 551-577... 

Hirabayashi, J., Kasai, K.l. The family of metazoan metal-independent P-galacto ide-binding lectins structure, function and molecular evolution. Glycohiology, 1993, 3, 297-304. 

These interactions involve adhesion proteins called selectins, which are found both on the rolling leukocytes and on the endothelial cells of the vascular walls. Selectins have a characteristic domain structure, consisting of an N-terminal extracellular lectin domain, a single epidermal growth factor (EGR) domain, a series of two to nine short consensus repeat (SCR) domains, a single transmembrane segment, and a short cytoplasmic domain. Lectin domains, first characterized in plants, bind carbohydrates... 

Binding proteins such as antibodies, receptors, and lectins may spontaneously aggregate in presence of bi- or multivalent specific ligands. This process, however, often results in assemblies that lack well-defined morphological and structural elements. 

Figure 47-10. Schematic diagram of the structure of human L-selectin. The extracellular portion contains an amino terminal domain homologous to C-type lectins and an adjacent epidermal growth factor-like domain. These are followed by a variable number of complement regulatory-like modules (numbered circles) and a transmembrane sequence (blackdiamond). A short cytoplasmic sequence (open rectangle) is at the carboxyl terminal. The structures of P- and E-selectin are similar to that shown except that they contain more complement-regulatory modules.The numbers of amino acids in L-, P-, and E- selectins, as deduced from the cDNA sequences, are 385,789, and 589, respectively. (Reproduced, with permission, from Bevilacqua MP, Nelson RM Selectins. J Clin Invest 1993 91 370.)...

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