A hinge region mutation in C1-inhibitor (Ala436-->Thr) results in nonsubstrate-like behavior and in polymerization of the molecule.

@article{Aulak1993AHR,
  title={A hinge region mutation in C1-inhibitor (Ala436-->Thr) results in nonsubstrate-like behavior and in polymerization of the molecule.},
  author={Kulwant S. Aulak and Eric Eldering and C. Erik Hack and Yvonne T P Lubbers and Richard A Harrison and Austin Mast and Marco Cicardi and Alvin E. Davis},
  journal={The Journal of biological chemistry},
  year={1993},
  volume={268 24},
  pages={18088-94}
}
C1-inhibitor(Mo), a dysfunctional C1-inhibitor molecule produced in two kindred with type II hereditary angioedema, has a mutation at the P10 position (Ala436 to Thr). Like most serpins with hinge region mutations (P14, P12, P10), C1-inhibitor(Mo) loses its inhibitory activity. However, unlike the other hinge region mutations, this mutant is not converted to a substrate. As shown by nondenaturing gel electrophoresis, gel filtration, sucrose density gradient ultracentrifugation, and electron… CONTINUE READING

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