Crystallography of serpins and serpin complexes.
作者： M.A. Dunstone , James C. Whisstock
DOI: 10.1016/B978-0-12-385950-1.00005-5
关键词:
摘要: The serpin superfamily of protease inhibitors undergoes a remarkable conformational change to inhibit target proteases. To date, over 80 different crystal structures have been determined. These data reveal that the monomer can adopt five conformations (native, partially inserted native, δ-form, latent, and cleaved). Further, recent studies also revealed serpins domain swap; biochemical suggest such an event underlies polymerization in diseases as antitrypsin deficiency. Here, we provide comprehensive analysis on crystallization context structural landscape superfamily.
elsevier.com
sci-hub.se 参考文章(100)
Hartmut Loebermann, Ryoji Tokuoka, Johann Deisenhofer, Robert Huber, Human α1-proteinase inhibitor: Crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function Journal of Molecular Biology. ,vol. 177, pp. 531- 557 ,(1984) , 10.1016/0022-2836(84)90298-5
H. Tonie Wright, Hua Xi Qian, Robert Huber, Crystal structure of plakalbumin, a proteolytically nicked form of ovalbumin Journal of Molecular Biology. ,vol. 213, pp. 513- 528 ,(1990) , 10.1016/S0022-2836(05)80212-8
Sheng Ye, Amy L. Cech, Ricardo Belmares, Robert C. Bergstrom, Youren Tong, David R. Corey, Michael R. Kanost, Elizabeth J. Goldsmith, The structure of a Michaelis serpin-protease complex. Nature Structural & Molecular Biology. ,vol. 8, pp. 979- 983 ,(2001) , 10.1038/NSB1101-979
Herbert Nar, Margit Bauer, Jean-Marie Stassen, Dietmar Lang, Ann Gils, Paul J Declerck, Plasminogen activator inhibitor 1. Structure of the native serpin, comparison to its other conformers and implications for serpin inactivation. Journal of Molecular Biology. ,vol. 297, pp. 683- 695 ,(2000) , 10.1006/JMBI.2000.3604
Stefano Ricagno, Sonia Caccia, Graziella Sorrentino, Giovanni Antonini, Martino Bolognesi, Human Neuroserpin: Structure and Time-Dependent Inhibition Journal of Molecular Biology. ,vol. 388, pp. 109- 121 ,(2009) , 10.1016/J.JMB.2009.02.056
U. Baumann, R. Huber, W. Bode, D. Grosse, M. Lesjak, C.B. Laurell, Crystal structure of cleaved human alpha 1-antichymotrypsin at 2.7 A resolution and its comparison with other serpins. Journal of Molecular Biology. ,vol. 218, pp. 595- 606 ,(1991) , 10.1016/0022-2836(91)90704-A
W. Li, T. E. Adams, J. Nangalia, C. T. Esmon, J. A. Huntington, Molecular basis of thrombin recognition by protein C inhibitor revealed by the 1.6-A structure of the heparin-bridged complex. Proceedings of the National Academy of Sciences of the United States of America. ,vol. 105, pp. 4661- 4666 ,(2008) , 10.1073/PNAS.0711055105
Jonathan Langdown, Klara J. Belzar, Wendy J. Savory, Trevor P. Baglin, James A. Huntington, The critical role of hinge-region expulsion in the induced-fit heparin binding mechanism of antithrombin. Journal of Molecular Biology. ,vol. 386, pp. 1278- 1289 ,(2009) , 10.1016/J.JMB.2009.01.028
Jan K. Jensen, Peter G.W. Gettins, High-resolution structure of the stable plasminogen activator inhibitor type-1 variant 14-1B in its proteinase-cleaved form: A new tool for detailed interaction studies and modeling Protein Science. ,vol. 17, pp. 1844- 1849 ,(2008) , 10.1110/PS.036707.108
Aiwu Zhou, Penelope E. Stein, James A. Huntington, Pasupathy Sivasothy, David A. Lomas, Robin W. Carrell, How Small Peptides Block and Reverse Serpin Polymerisation Journal of Molecular Biology. ,vol. 342, pp. 931- 941 ,(2004) , 10.1016/J.JMB.2004.07.078