Structures and functions associated with the group of mammalian lectins containing collagen‐like sequences
- 19 June 1989
- journal article
- review article
- Published by Wiley in FEBS Letters
- Vol. 250 (1), 78-84
- https://doi.org/10.1016/0014-5793(89)80689-1
Abstract
The number of proteins found in body fluids and at cell surfaces, which are known to display carbohydrate‐binding properties, continues to increase rapidly. In these proteins, in addition to a domain associated with lectin properties, one or more, non‐lectin domains are present. It is possible that binding of sugar residues by the lectin domain may be important in triggering a variety of recognition and clearance mechanisms via the non‐lectin domains. The group of lectins containing collagen‐like sequences may provide some insight into structure/function relationships of the different domains in view of the well defined structures already available for several of these molecules.This publication has 16 references indexed in Scilit:
- A human serum mannose-binding protein inhibits in vitro infection by the human immunodeficiency virus.The Journal of Experimental Medicine, 1989
- The Clq receptorMolecular Immunology, 1988
- Macromolecular organization of natural and recombinant lung surfactant protein SP 28–36Journal of Molecular Biology, 1988
- The binding site for C1q on IgGNature, 1988
- Ultrastructure and composition of bovine conglutininBiochemical Journal, 1986
- Isolation and characterization of the human pulmonary surfactant apoprotein geneNature, 1985
- Biological significance of carbohydrate chains on monoclonal antibodies.Proceedings of the National Academy of Sciences, 1983
- What should be called a lectin?Nature, 1980
- The Role of Surface Carbohydrates in the Hepatic Recognition and Transport of Circulating GlycoproteinsPublished by Wiley ,1974