Viper venom disintegrins and related molecules.

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  • Author(s): McLane MA;McLane MA; Marcinkiewicz C; Vijay-Kumar S; Wierzbicka-Patynowski I; Niewiarowski S
  • Source:
    Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine (New York, N.Y.) [Proc Soc Exp Biol Med] 1998 Nov; Vol. 219 (2), pp. 109-19.
  • 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 Science [etc.] Country of Publication: United States NLM ID: 7505892 Publication Model: Print Cited Medium: Print ISSN: 0037-9727 (Print) Linking ISSN: 00379727 NLM ISO Abbreviation: Proc Soc Exp Biol Med Subsets: MEDLINE
    • Publication Information:
      Original Publication: Malden, MA [etc.] Blackwell Science [etc.]
    • Subject Terms:
      Disintegrins*/chemistry ; Disintegrins*/metabolism ; Platelet Aggregation Inhibitors*/chemistry ; Platelet Aggregation Inhibitors*/metabolism ; Viper Venoms*; Amino Acid Sequence ; Animals ; Dimerization ; Endopeptidases/chemistry ; Endopeptidases/metabolism ; Humans ; Molecular Sequence Data ; Sequence Alignment
    • Abstract:
      The term "disintegrin" was first used in 1990 to describe a group of viper venom-derived, nonenzymatic small proteins that shared numerous structural and functional properties. These proteins, which have been found in a great number of viper species studied since that time possess both a remarkable sequence homology and an equally notable variability in potency and selectivity in their interactions with integrin receptors. The discovery that small disintegrins may actually have been derived from much larger mosaic proteins possessing catalytic activity, and that species other than snakes (both plant and animal) produce proteins containing disintegrin-like domains, has led to much research related to both the proteins themselves and the receptors to which they bind. The purpose of this review is to discuss the literature and the authors' own data on the structure and function of disintegrins and their relevance to the studies on proteins containing disintegrin-like domains, such as hemorrhagins and ADAMs.
    • Number of References:
      103
    • Grant Information:
      DE 11844 United States DE NIDCR NIH HHS; HL 45486 United States HL NHLBI NIH HHS
    • Accession Number:
      0 (Disintegrins)
      0 (Platelet Aggregation Inhibitors)
      0 (Viper Venoms)
      EC 3.4.- (Endopeptidases)
      EC 3.4.- (hemorrhagic proteinase IV)
    • Publication Date:
      Date Created: 19981028 Date Completed: 19981110 Latest Revision: 20200930
    • Publication Date:
      20250114
    • Accession Number:
      10.3181/00379727-219-44322
    • Accession Number:
      9790167