alexa Structural and functional aspects of C1-inhibitor.


Journal of Hematology & Thromboembolic Diseases

Author(s): Bos IG, Hack CE, Abrahams JP

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Abstract C1-Inh is a serpin that inhibits serine proteases from the complement and the coagulation pathway. C1-Inh consists of a serpin domain and a unique N-terminal domain and is heavily glycosylated. Non-functional mutants of C1-Inh can give insight into the inhibitory mechanism of C1-Inh. This review describes a novel 3D model of C1-Inh, based on a newly developed homology modelling method. This model gives insight into a possible potentiation mechanism of C1-Inh and based on this model the essential residues for efficient inhibition by C1-Inh are discussed.
This article was published in Immunobiology and referenced in Journal of Hematology & Thromboembolic Diseases

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