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Methods for Determining and Understanding Serpin Structure and Function: X-Ray Crystallography

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Serpins

Part of the book series: Methods in Molecular Biology ((MIMB,volume 1826))

Abstract

Deciphering the X-ray crystal structures of serine protease inhibitors (serpins) and serpin complexes has been an integral part of understanding serpin function and inhibitory mechanisms. In addition, high-resolution structural information of serpins derived from the three domains of life (bacteria, archaea, and eukaryotic) and viruses has provided valuable insights into the hereditary and evolutionary history of this unique superfamily of proteins. This chapter will provide an overview of the predominant biophysical method that has yielded this information, X-ray crystallography. In addition, details of up-and-coming methods, such as neutron crystallography, cryo-electron microscopy, and small- and wide-angle solution scattering, and their potential applications to serpin structural biology will be briefly discussed. As serpins remain important both biologically and medicinally, the information provided in this chapter will aid in future experiments to expand our knowledge of this family of proteins.

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Authors and Affiliations

  1. Laboratory of Chemical Physics, National Institutes of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, USA

    Brian P. Mahon

  2. Department of Biochemistry and Molecular Biology, University of Florida College of Medicine, Gainesville, FL, USA

    Robert McKenna

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  1. Brian P. Mahon
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  2. Robert McKenna
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Correspondence to Brian P. Mahon .

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Editors and Affiliations

  1. Biodesign Center for Personalized Diagnostics and Center for Immunotherapy Vaccines and Virotherapy, Arizona State University, Tempe, AZ, USA

    Alexandra Lucas

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Mahon, B.P., McKenna, R. (2018). Methods for Determining and Understanding Serpin Structure and Function: X-Ray Crystallography. In: Lucas, A. (eds) Serpins. Methods in Molecular Biology, vol 1826. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-8645-3_2

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  • DOI: https://doi.org/10.1007/978-1-4939-8645-3_2

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