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πŒΌπŒ°πŒΏπ‚πŒ²πŒΏπƒ πƒπŒΊπŒ΄πŒΉπ‚πŒ΄πŒΉπŒ½πƒ

πƒπŒΊπŒ΄πŒΉπ‚πŒ΄πŒΉπŒ½πƒ
English: The native state of serpins is an equilibrium between a fully-stressed state (left) and a partially relaxed state (right). The five-stranded A-sheet (light blue) contains two functionally important regions for the serpin's mechanism, the breach and the shutter. The Reactive Centre Loop (RCL, blue) exists in a dynamic equilibrium between the fully exposed conformation (left) and a conformation where it is partially inserted into the breach of the A-sheet (right). (PDB: 1QLP, 1YXA​). [1] [2]
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πŒ±π‰πŒΊπŒ°π‚πŒ΄πŒΉπƒ Thomas Shafee

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  1. ↑ Elliott PR, Lomas DA, Carrell RW, Abrahams JP. (1996). "Inhibitory conformation of the reactive loop of alpha 1-antitrypsin". Nature Structural & Molecular Biology 3 (8): 676–81. DOI:10.1038/nsb0896-676. PMID 8756325.
  2. ↑ (2005). "The murine orthologue of human antichymotrypsin: a structural paradigm for clade A3 serpins.". J Biol Chem 280 (52): 43168–78. DOI:10.1074/jbc.M505598200. PMID 16141197.

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