Chapter title |
Methods for Determining and Understanding Serpin Structure and Function: X-Ray Crystallography
|
---|---|
Chapter number | 2 |
Book title |
Serpins
|
Published in |
Methods in molecular biology, September 2018
|
DOI | 10.1007/978-1-4939-8645-3_2 |
Pubmed ID | |
Book ISBNs |
978-1-4939-8644-6, 978-1-4939-8645-3
|
Authors |
Brian P. Mahon, Robert McKenna, Mahon, Brian P., McKenna, Robert |
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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