Serpins and other covalent protease inhibitors

Current Opinion in Structural Biology

Volumn 11, Issue 6, 2001, Pages 740-745

  Ye, Sheng ^a   Goldsmith, Elizabeth J ^a  

^a UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA 1 ANTITRYPSIN; CASPASE 8; CYSTEINE PROTEINASE; PROTEIN P35; PROTEINASE INHIBITOR; SERINE PROTEINASE INHIBITOR; TRYPSIN; TRYPSIN INHIBITOR;

COMPLEX FORMATION; COVALENT BOND; CRYSTAL STRUCTURE; DRUG CONFORMATION; DRUG MECHANISM; LEPIDOPTERA; MICHAELIS CONSTANT; NONHUMAN; PRIORITY JOURNAL; REVIEW;

LEPIDOPTERA; MANDUCA SEXTA;

EID: 0035692792     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(01)00275-5     Document Type: Review

References (48)

1. The serpins are an expanding superfamily of structurally similar but functionally diverse proteins: Evolution, mechanism of inhibition, novel functions, and a revised nomenclature
2. Conformational properties of serine proteinase inhibitors (serpins) confer multiple pathophysiological roles
3. Phylogeny of the serpin superfamily: Implications of patterns of amino acid conservation for structure and function
4. Familial dementia caused by polymerization of mutant neuroserpin
5. What do dysfunctional serpins tell us about molecular mobility and disease
6. Structure-function relationships in serpins: Current concepts and controversies
7. An atlas of serpin conformations
8. The structural puzzle of how serpin serine proteinase inhibitors work
9. Implications of the three-dimensional structure of α1-antitrypsin for structure and function of serpins
10. Partitioning of serpin-proteinase reactions between stable inhibition and substrate cleavage is regulated by the rate of serpin reactive center loop insertion into β-sheet A
11. Structural basis of latency in plasminogen activator inhibitor-1
12. The 2.6 Å structure of antithrombin indicates a conformational change at the heparin binding site
13. Structure of a serpin-protease complex shows inhibition by deformation
14. Structural basis for serpin inhibitor activity
15. Evidence for an ester bond between thrombin and heparin cofactor
16. Serpin-protease complexes are trapped as stable acyl-enzyme intermediates
17. An ester bond linking a fragment of a serine proteinase to its serpin inhibitor
18. Crystal structure of an uncleaved serpin reveals the conformation of an inhibitory reactive loop
19. Crystal structure of an uncleaved α1-antitrypsin reveals the conformation of its inhibitory reactive loop
20. Wild-type α1-antitrypsin is in the canonical inhibitory conformation
21. The structure of active serpin 1K from Manduca sexta
22. Human α1-proteinase inhibitor. Crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function
23. Crystal structure of cleaved equine leucocyte elastase inhibitor determined at 1.95 Å resolution
24. Immunologic evidence for insertion of the reactive-bond loop of antithrombin into the A β-sheet of the inhibitor during the trapping of target proteinases
25. Formation of the covalent serpin proteinase complex involves translocation of the proteinase by more than 70 Å and full insertion of the reactive center loop into β-sheet A
26. The structure of a serpin-protease complex revealed by intramolecular distance measurements using donor-donor energy migration and mapping of interaction sites
27. Trypsin complexed with α1-proteinase inhibitor has an increased structural flexibility
28. Structural change in α-chymotrypsin induced by complexation with α1-antichymotrypsin as seen by enhanced sensitivity to proteolysis
29. The serpin inhibitory mechanism is critically dependent on the length of the reactive center loop
30. Crystal structure of viral serpin crmA provides insights into its mechanism of cysteine proteinase inhibition
31. Crystal structure of the apoptotic suppressor CrmA in its cleaved form
32. The structure of a Michaelis serpin-protease complex
33. Kinetic characterization of the proteinase binding defect in a reactive site variant of the serpin, antithrombin. Role of the P1′ residue in transition-state stabilization of antithrombin-proteinase complex formation
34. Serpin-resistant mutants of human tissue-type plasminogen activator
35. Two distinct urokinase-serpin interactions regulate the initiation of cell surface-associated plasminogen activation
36. High-density mutagenesis by combined DNA shuffling and phage display to assign essential amino acid residues in protein-protein interactions: Application to study structure-function of plasminogen activation inhibitor 1 (PAI-1)
37. Plasma serine proteinase inhibitors (serpins) exhibit major conformational changes and a large increase in conformational stability upon cleavage at their reactive sites
38. Endothelial cells produce a latent inhibitor of plasminogen activators that can be activated by denaturants
39. Kinetically controlled folding of the serpin plasminogen activator inhibitor-1
40. Effects of serpin binding on the target proteinase: Global stabilization, localized increased structural flexibility, and conserved hydrogen bonding at the active site
41. Contact order, transition state placement and the refolding rates of single domain proteins
42. Crystal structure of baculovirus p35: Role of a novel reactive site loop in apoptotic caspase inhibition
43. Covalent inhibition revealed by the crystal structure of the caspase-8/p35 complex
44. Crystal structure of baculovirus p35 reveals a novel conformational change in the reactive site loop after caspase cleavage
45. Apoptotic suppression by baculovirus p35 involves cleavage by and inhibition of a virus-induced CED-3/ICE-like protease
46. Influenza hemagglutinin is spring-loaded by a metastable native conformation
47. The three-dimensional structure of caspase-8: An initiator enzyme in apoptosis