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The C-type lectin superfamily in the immune system.

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  • Author(s): Weis WI;Weis WI; Taylor ME; Drickamer K
  • Source:
    Immunological reviews [Immunol Rev] 1998 Jun; Vol. 163, pp. 19-34.
  • Publication Type:
    Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.; Review
  • Language:
    English
  • Additional Information
    • Source:
      Publisher: Blackwell Country of Publication: England NLM ID: 7702118 Publication Model: Print Cited Medium: Print ISSN: 0105-2896 (Print) Linking ISSN: 01052896 NLM ISO Abbreviation: Immunol Rev Subsets: MEDLINE
    • Publication Information:
      Publication: <2002-> : Oxford : Blackwell
      Original Publication: Copenhagen, Munksgaard.
    • Subject Terms:
      Calcium* ; Lectins, C-Type* ; Mannose-Binding Lectins* ; Protein Conformation*; Lectins/*chemistry; Amino Acid Sequence ; Animals ; Carrier Proteins/chemistry ; Carrier Proteins/metabolism ; Collectins ; Humans ; Immune System/metabolism ; Killer Cells, Natural/metabolism ; Lectins/metabolism ; Mannose Receptor ; Molecular Sequence Data ; Receptors, Cell Surface/chemistry ; Receptors, Cell Surface/metabolism ; Receptors, Immunologic/chemistry ; Selectins/metabolism
    • Abstract:
      Protein-carbohydrate interactions serve multiple functions in the immune system. Many animal lectins (sugar-binding proteins) mediate both pathogen recognition and cell-cell interactions using structurally related Ca(2+)-dependent carbohydrate-recognition domains (C-type CRDs). Pathogen recognition by soluble collections such as serum mannose-binding protein and pulmonary surfactant proteins, and also the macrophage cell-surface mannose receptor, is effected by binding of terminal monosaccharide residues characteristic of bacterial and fungal cell surfaces. The broad selectivity of the monosaccharide-binding site and the geometrical arrangement of multiple CRDs in the intact lectins explains the ability of the proteins to mediate discrimination between self and non-self. In contrast, the much narrower binding specificity of selectin cell adhesion molecules results from an extended binding site within a single CRD. Other proteins, particularly receptors on the surface of natural killer cells, contain C-type lectin-like domains (CTLDs) that are evolutionarily divergent from the C-type lectins and which would be predicted to function through different mechanisms.
    • Number of References:
      73
    • Grant Information:
      GM50565 United States GM NIGMS NIH HHS; United Kingdom Wellcome Trust
    • Accession Number:
      0 (Carrier Proteins)
      0 (Collectins)
      0 (Lectins)
      0 (Lectins, C-Type)
      0 (Mannose Receptor)
      0 (Mannose-Binding Lectins)
      0 (Receptors, Cell Surface)
      0 (Receptors, Immunologic)
      0 (Selectins)
      SY7Q814VUP (Calcium)
    • Publication Date:
      Date Created: 19980813 Date Completed: 19981106 Latest Revision: 20220318
    • Publication Date:
      20250114
    • Accession Number:
      10.1111/j.1600-065x.1998.tb01185.x
    • Accession Number:
      9700499