Serpins: implications of a mobile reactive centre.
The serpins are unique among the families of serine proteinase inhibitors in having a reactive centre that is situated on a mobile loop. The structures of three alternative conformations are now known, and it can be deduced that the active form involves the partial insertion of the loop into the A sheet of the molecule. The ability of the loop to move in and out of this sheet has been adapted by evolution to allow the modulation of inhibitory activity. Manipulation of the structure of the loop and of other functional domains in the serpin superfamily enables the production of serpins with tailor-made activities. The ability of the loop to lock in latent conformations or to take part in intermolecular polymerization has implications for the production and stabilization of recombinant serpins. This review has been adapted from Current Opinion in Structural Biology 1992, 2:438-446.
Haematology Department, University of Cambridge, UK.
D C
DC
Crowther
D L
DL
Evans
R W
RW
Carrell
D000595:Amino Acid Sequence; D001709:Biotechnology; D008969:Molecular Sequence Data; D011487:Protein Conformation; D016415:Sequence Alignment; D015843:Serpins / Q000737:chemistry / Q000378:metabolism*
D015843:Serpins