A model for hydrophobic protrusions on peripheral membrane proteins.

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  • Author(s): Fuglebakk E;Fuglebakk E;Fuglebakk E; Reuter N; Reuter N; Reuter N
  • Source:
    PLoS computational biology [PLoS Comput Biol] 2018 Jul 26; Vol. 14 (7), pp. e1006325. Date of Electronic Publication: 2018 Jul 26 (Print Publication: 2018).
  • Publication Type:
    Journal Article; Research Support, Non-U.S. Gov't
  • Language:
    English
  • Additional Information
    • Source:
      Publisher: Public Library of Science Country of Publication: United States NLM ID: 101238922 Publication Model: eCollection Cited Medium: Internet ISSN: 1553-7358 (Electronic) Linking ISSN: 1553734X NLM ISO Abbreviation: PLoS Comput Biol Subsets: MEDLINE
    • Publication Information:
      Original Publication: San Francisco, CA : Public Library of Science, [2005]-
    • Subject Terms:
      Models, Biological*; Amino Acids/*metabolism ; Membrane Proteins/*metabolism; Amino Acids/analysis ; Binding Sites ; Datasets as Topic ; Hydrophobic and Hydrophilic Interactions ; Membrane Proteins/chemistry ; Protein Binding
    • Abstract:
      With remarkable spatial and temporal specificities, peripheral membrane proteins bind to biological membranes. They do this without compromising solubility of the protein, and their binding sites are not easily distinguished. Prototypical peripheral membrane binding sites display a combination of patches of basic and hydrophobic amino acids that are also frequently present on other protein surfaces. The purpose of this contribution is to identify simple but essential components for membrane binding, through structural criteria that distinguish exposed hydrophobes at membrane binding sites from those that are frequently found on any protein surface. We formulate the concepts of protruding hydrophobes and co-insertability and have analysed more than 300 families of proteins that are classified as peripheral membrane binders. We find that this structural motif strongly discriminates the surfaces of membrane-binding and non-binding proteins. Our model constitutes a novel formulation of a structural pattern for membrane recognition and emphasizes the importance of subtle structural properties of hydrophobic membrane binding sites.
      Competing Interests: The authors have declared that no competing interests exist.
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    • Accession Number:
      0 (Amino Acids)
      0 (Membrane Proteins)
    • Publication Date:
      Date Created: 20180727 Date Completed: 20190114 Latest Revision: 20190114
    • Publication Date:
      20240104
    • Accession Number:
      PMC6080788
    • Accession Number:
      10.1371/journal.pcbi.1006325
    • Accession Number:
      30048443