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Animal Lectins: Form, Function and Clinical Applications pp 331–347Cite as

Mannose Receptor Family: R-Type Lectins

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Abstract

R-type lectins exist ubiquitously in nature and mainly bind to galactose unit of sugar chains. Originally found in plant lectin, Ricin, the R-type lectin domain is found in several animal lectins, including the members of mannose receptor (MR) family, and in some invertebrate lectins (discussed in Chap. 14). The R-type domain contained in these proteins is the CRD, which is also termed a carbohydrate-binding module (CBM) and has been placed in the CBM13 family in the CAZy database (carbohydrate-active enzymes database). While the A chain in ricin has eight α-helices and eight β-strands, and is the catalytic subunit, the B chain contains R-type lectin domains, has two tandem CRDs that are about 35 Å apart and have a shape resembling a barbell, with one binding domain at each end. Each R-type domain has a three-lobed organization that is a β-trefoil structure (from the Latin trifolium meaning “three-leaved plant”). The β-trefoil structure probably arose evolutionarily through gene fusion events linking a 42-amino-acid peptide subdomain that has galactose-binding activity. The three lobes are termed α, β, and γ and are arranged around a threefold axis. Conceivably, each lobe could be an independent binding site, but in most R-type lectins only one or two of these lobes retain the conserved amino acids required for sugar binding. The R-type domain is also found in pierisin-1, which is a cytotoxic protein from the cabbage butterfly Pieris rapae, and in the homologous protein pierisin-2, from Pieris brassicae. Tandem R-type motifs are found in some other R-type family members. For example, Limulus horseshoe crab coagulation factor G has a central R-type lectin domain, which is flanked at the amino terminus by a xylanase Z-like domain and at the carboxyl terminus by a glucanase-like domain. In this chapter we will restrict our discussion to R-type lectins of mannose receptor family, which comprises also of endocytic receptors.

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Authors and Affiliations

  1. Vaccine Production Division, Panacea Biotec, Lalru (Mohali), Punjab, India

    Rajesh K. Gupta (General Manager)

  2. Department of Biophysics, Punjab University, Chandigarh, India

    G. S. Gupta (Former Professor and Chairman)

Authors
  1. Rajesh K. Gupta
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  2. G. S. Gupta
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© 2012 Springer-Verlag Wien

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Gupta, R.K., Gupta, G.S. (2012). Mannose Receptor Family: R-Type Lectins. In: Animal Lectins: Form, Function and Clinical Applications. Springer, Vienna. https://doi.org/10.1007/978-3-7091-1065-2_15

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