C1 inhibitor hinge region mutations produce dysfunction by different mechanisms

@article{Davis1992C1IH,
  title={C1 inhibitor hinge region mutations produce dysfunction by different mechanisms},
  author={Alvin E. Davis and Kulwant Singh Aulak and Richard B. Parad and Hilary P. Stecklein and Eric Eldering and C. Erik Hack and Judith Kramer and Robert C Strunk and John J. Bissler and Fred S. Rosen},
  journal={Nature Genetics},
  year={1992},
  volume={1},
  pages={354-358}
}
Heterozygosity for a mutant dysfunctional C1 inhibitor protein, a member of the serine proteinase inhibitor (serpin) superfamily, results in type II hereditary angioneurotic oedema. We identified a “hinge” region mutation in C1 inhibitor with a Val to Glu replacement at P14 Val–432. Recombinant C1 inhibitors P10 Ala→Thr and P14 Val→Glu did not form stable complexes with fluid phase C1s or kallikrein. The P14 Val→Glu mutant, however, was cleaved to a 96K form by C1s, while the P10 Ala→Thr mutant… 
Characterization of C1 Inhibitor-Ta
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TLDR
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TLDR
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TLDR
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TLDR
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TLDR
A large number of new mutations related to HAE are identified providing additional evidence of the genetic heterogeneity of this disease and point toward particular amino acid residues important for protein function that may represent mutation hot spots.
Crucial residues in the carboxy-terminal end of C1 inhibitor revealed by pathogenic mutants impaired in secretion or function.
TLDR
Data point to a key role of certain residues in the conserved COOH-terminal region of serpins in determining the protein foldings compatible with transport and proper exposure of the reactive site loop in angioedema patients.
Structure and function of C1-inhibitor.
C1-INH belongs to the family of serpins. Structural studies have yielded a clear understanding of the biochemical principle underlying the functional activities of these proteins. Although the
Pathogenetic and clinical aspects of C1 inhibitor deficiency.
TLDR
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Effect of reactive site loop elongation on the inhibitory activity of C1-inhibitor.
TLDR
It is suggested that the relatively weak inhibitory activity of C1-Inh is not the result of its short RSL, which has, surprisingly, the optimal length for inhibition.
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TLDR
The deletion of nucleotides encoding Lys-251 (AAG) in C1 inhibitor Ta, the dysfunctional C1 inhibitors from a family with type II hereditary angioneurotic edema, is described and it is suggested that this deletion creates a new glycosylation site on SDS/PAGE and very likely interferes with protein function.
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TLDR
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TLDR
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TLDR
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TLDR
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