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1. Introduction
2. The serpin superfamily
3. Extent of the family
4. Diversity of function
5. Human serpins
6. Serpins, a field driven by structural biology
7. 1984: the structure of cleaved alpha-1-antitrypsin
8. 1991: the structure of ovalbumin
9. 1996: the structure of native antitrypsin
10. Serpins fold to a metastable state
11. Role of the serpin conformational change
12. Serpin conservation and conformational change
13. Why so complex?
14. Antithrombin, heparin, and thrombin / factor Xa
15. PAI-1 and the latent form
16. The cost of complexity
17. Alpha-1-antitrypsin deficiency
18. Polymers of antitrypsin (1)
19. Polymers of antitrypsin (2)
20. Loop sheet polymerisation
21. Model of a loop sheet polymer
22. Studies in support of A-sheet polymerisation
23. Mining serpin variation
24. The number of serpinopathies continues to grow
25. Polymerogenic mutations tend to cluster
26. Antithrombin Rouen VI
27. Neuroserpin and FENIB
28. Alpha-1-antichymotrypsin
29. Delta-antichymotrypsin
30. Strategies to prevent serpin polymerisation
31. Stabilising the native serpin fold
32. Conclusions
33. Acknowledgments
34. References (1)
35. References (2)
36. References (3)
37. References (4)

Topics Covered

• Serpins
• Proteases
• Serpin function
• Serpin structure
• Serpin protease interactions
• Role of co-factors in serpin function
• Serpin polymerization and dysfunction
• Antitrypsin deficiency
• Z-antitrypsin
• Mechanism of serpin polymerization
• Other serpin deficiencies
• Antithrombin deficiency
• Neuroserpin polymerization
• Antichymotrypsin deficiency
• Approaches to combat serpinopathies

Links

Series:

• Protein Epidemiology

Categories:

• Biochemistry
• Cell Biology
• Clinical Practice

Therapeutic Areas:

• Haematology

Talk Citation

Publication History

• Published on October 1, 2007
• Archived on August 13, 2020

Financial Disclosures

• Dr. James Whisstock has not informed HSTalks of any commercial/financial relationship that it is appropriate to disclose.