How the serpin α1-proteinase inhibitor folds.

The Journal of Biological Chemistry
Klavs Dolmer, Peter G W Gettins

Abstract

Serpins are remarkable and unique proteins in being able to spontaneously fold into a metastable conformation without the aid of a chaperone or prodomain. This metastable conformation is essential for inhibition of proteinases, so that massive serpin conformational change, driven by the favorable energetics of relaxation of the metastable conformation to the more stable one, can kinetically trap the proteinase-serpin acylenzyme intermediate. Failure to direct folding to the metastable conformation would lead to inactive, latent serpin. How serpins fold into such a metastable state is unknown. Using the ability of component peptides from the serpin α(1)PI to associate, we have now elucidated the pathway by which this serpin efficiently folds into its metastable state. In addition we have established the likely structure of the polymerogenic intermediate of the Z variant of α(1)PI.

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Citations

Oct 18, 2014·Nature Chemical Biology·Anne GershensonSheena E Radford
May 26, 2016·Proceedings of the National Academy of Sciences of the United States of America·Kshama ChandrasekharDaniel N Hebert
Jul 23, 2014·Angewandte Chemie·Morten B TrelleThomas J D Jørgensen
Nov 13, 2019·The Journal of Biological Chemistry·Anne GershensonPatrick L Wintrode
Jun 2, 2016·The Journal of Biological Chemistry·Xin HuangAiwu Zhou
Jul 30, 2016·The Biochemical Journal·Peter G W Gettins, Steven T Olson
Feb 27, 2020·International Journal of Molecular Sciences·Esra Karatas, Marion Bouchecareilh
Oct 23, 2020·Science Advances·Sarah V FaullDavid A Lomas
Feb 2, 2021·The Journal of Biological Chemistry·Anne GershensonPatrick L Wintrode

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