The primary role of the P1 residue (ser359) of alpha-1-proteinase inhibitor

Biochemical and Biophysical Research Communications
N MathesonJ Travis

Abstract

The replacement of ser359 with ala359 at the P1 position in human alpha-1-proteinase inhibitor results in the production of a variant protein containing 15% of the inhibitory activity of the normal inhibitor. Separation of active from inactive inhibitor on anhydrochymotrypsin-sepharose yields a form which has a second order association rate with neutrophil elastase which is approximately one half that for the native protein. These data indicate that the P1 residue is not of primary importance during the interaction of proteinases with alpha-1-proteinase inhibitor. Since substitution of alanine for serine causes the formation, primarily, of inactive inhibitor the major function of ser359 probably involves proper folding to give a functionally active inhibitory conformation.

References

Feb 24, 1976·Biochemistry·R J Baugh, J Travis
Jan 1, 1983·Annual Review of Biochemistry·J Travis, G S Salvesen

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Citations

Aug 26, 2011·Molecular Immunology·Alberto López-LeraMargarita López-Trascasa
Jul 24, 2001·The Journal of Immunology : Official Journal of the American Association of Immunologists·R ZahediA E Davis

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