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Proteases universally recognize beta strands in their active sites

Chemical Reviews, ISSN: 0009-2665, Vol: 105, Issue: 3, Page: 973-999
2005
  • 364
    Citations
  • 0
    Usage
  • 187
    Captures
  • 5
    Mentions
  • 0
    Social Media
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Metrics Details

  • Citations
    364
  • Captures
    187
  • Mentions
    5
    • References
      4
      • Wikipedia
        4
    • News Mentions
      1
      • News
        1

Most Recent News

Structural basis of broad-spectrum β-lactam resistance in Staphylococcus aureus

Nature, Published online: 04 January 2023; doi:10.1038/s41586-022-05583-3 Cryo-electron microscopy structures of Staphylococcus aureus BlaR1 reveal dynamic signalling states regulating broad spectrum β-lactam antibiotic resistance through cleavage of the transcriptional repressor BlaI and induced expression of the β-lactamase blaZ and the β-lactam-resistant cell-wall transpeptidase mecA.

Review Description

One way to combat infectious diseases is to selectively inhibit foreign proteases within host cells, thus retarding replication rates of infectious organisms and assisting normal immunological defense mechanisms involved in their eradication. This review gives a summary of over 1500 three dimensional crystal (X-ray) and solution (NMR) structures from the pdb of substrates, products and inhibitors bound in the active sites of aspartic, serine, metallo, cysteine, and threonine endopeptidases. These active sites of all five protease classes recognize peptidic and non-peptidic ligands in an extended beta strand conformation, with few exceptions. Comparisons of protease-bound ligand conformations are illustrated by structural superpositions for a subset of structures, including 21 aspartic, 44 serine, 20 metallo, 23 cysteine, and 2 threonine proteases, among the protease-ligand structures analyzed. The extended substrate-binding mode is also illustrated for 3 aspartic proteases, 1 serine protease, 1 cysteine protease and 1 metalloprotease.

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