Taxonomic distribution of proteins containing CLECT domains

The CLECT domain within your query sequence starts at position 97 and ends at position 208, and its E-value is 1.68e-17.

Lectin-carbohydrate interactions: different folds, common recognition principles.

Elgavish S, Shaanan B
Trends Biochem Sci. 1997; 22: 462-7

Lectins can be found in many organisms and are involved in a multitude of cellular processes that depend on specific recognition of complex carbohydrates. The stereochemical principles underlying the recognition process have been the subject of extensive biochemical and structural studies. When examined from the viewpoint of the bound sugar, the structural information accumulated so far on lectins and other proteins that are specific to galactose and glucose (or mannose), provides suggestive evidence for distinct ligand-dependent distribution of hydrogen-bond partners in the combining site.

Structural basis of lectin-carbohydrate recognition.

Weis WI, Drickamer K
Annu Rev Biochem. 1996; 65: 441-73

Lectins are responsible for cell surface sugar recognition in bacteria, animals, and plants. Examples include bacterial toxins; animal receptors that mediate cell-cell interactions, uptake of glycoconjugates, and pathogen neutralization; and plant toxins and mitogens. The structural basis for selective sugar recognition by members of all of these groups has been investigated by x-ray crystallography. Mechanisms for sugar recognition have evolved independently in diverse protein structural frameworks, but share some key features. Relatively low affinity binding sites for monosaccharides are formed at shallow indentations on protein surfaces. Selectivity is achieved through a combination of hydrogen bonding to the sugar hydroxyl groups with van der Waals packing, often including packing of a hydrophobic sugar face against aromatic amino acid side chains. Higher selectivity of binding is achieved by extending binding sites through additional direct and water-mediated contacts between oligosaccharides and the protein surface. Dramatically increased affinity for oligosaccharides results from clustering of simple binding sites in oligomers of the lectin polypeptides. The geometry of such oligomers helps to establish the ability of the lectins to distinguish surface arrays of polysaccharides in some instances and to crosslink glycoconjugates in others.

Collectins: collagenous C-type lectins of the innate immune defense system.

Holmskov U, Malhotra R, Sim RB, Jensenius JC
Immunol Today. 1994; 15: 67-74

Collectins are humoral lectins found in mammals and birds. They are oligomers whose subunits comprise three polypeptide chains each containing a collagenous section and a C-terminal lectin domain. They are related structurally and functionally to the first component of the classical complement pathway, C1q, and seem to serve important roles in innate immunity through opsonization and complement activation. The lectin domains bind carbohydrates on microorganisms, while the collagenous regions are ligands for the collectin receptor on phagocytes and also mediate C1q-independent activation of the classical complement pathway.

Two distinct classes of carbohydrate-recognition domains in animal lectins.

Drickamer K
J Biol Chem. 1988; 263: 9557-60