Crystal structure of the apoptotic suppressor CrmA in its cleaved form

Structure

Volumn 8, Issue 7, 2000, Pages 789-797

  Renatus, Martin ^a   Zhou, Qiao ^a,b   Stennicke, Henning R ^a   Snipas, Scott J ^a   Turk, Dušan ^c   Bankston, Laurie A ^d   Liddington, Robert C ^d   Salvesen, Guy S ^a  

^a BURNHAM INSTITUTE   (United States)

^b HARVARD MEDICAL SCHOOL   (United States)

^c JO EF STEFAN INSTITUTE   (Slovenia)

^d Extracellular Matrix Biol B   (United States)

Author keywords

Apoptosis; Caspase; Protease; Protease inhibitor; Serpin; Viral countermeasures

Indexed keywords

CASPASE; ENZYME INHIBITOR; INTERLEUKIN 18; INTERLEUKIN 1BETA; PROTEINASE;

AMINO TERMINAL SEQUENCE; APOPTOSIS; ARTICLE; COWPOX VIRUS; CRYSTAL STRUCTURE; INFLAMMATION; MOLECULAR RECOGNITION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN EXPRESSION;

COWPOX VIRUS;

EID: 0034661477     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(00)00165-9     Document Type: Article

References (49)

1. Salvesen G.S., Dixit V.M. Caspases: intracellular signaling by proteolysis. Cell. 91:1997;443-446.
2. Thornberry N.A., Lazebnik Y. Caspases: enemies within. Science. 281:1998;1306-1312.
3. Ray C.A., Pickup D.J.et al. Viral inhibition of inflammation: cowpox virus encodes an inhibitor of the interleukin-1β-converting enzyme. Cell. 69:1992;597-604.
4. Zhou Q., Snipas S., Orth K., Dixit V.M., Salvesen G.S. Target protease specififity of the viral serpin CrmA: analysis of five caspases. J. Biol. Chem. 273:1997;7797-7800.
5. Walsh C.M., Wen B.G., Chinnaiyan A.M., O'Rourke K., Dixit V.M., Hedrick S.M. A role for FADD in T cell activation and development. Immunity. 8:1998;439-449.
6. Komiyama T., Salvesen G.et al. Inhibition of interleukin-1beta converting enzyme by the cowpox virus serpin CrmA. An example of cross-class inhibition. J. Biol. Chem. 269:1994;19331-19337.
7. Turner S., Kenshole B., Ruby J. Viral modulation of the host response via crmA/SPI-2 expression. Immunol. Cell Biol. 77:1999;236-241.
8. Pickup D.J., Ink B.S., Hu W., Ray C.A., Joklik W.K. Hemorrhage in lesions caused by cowpox virus is induced by a viral protein that is related to plasma protein inhibitors of serine proteases. Proc. Natl Acad. Sci. USA. 83:1986;7698-7702.
9. Potempa J., Korzus E., Travis J. The serpin superfamily of proteinase inhibitors: structure, function, and regulation. J. Biol. Chem. 269:1994;15957-15960.
10. Quan L.T., Caputo A., Bleackley R.C., Pickup D.J., Salvesen G.S. Granzyme B is inhibited by the cowpox virus serpin CrmA. J. Biol. Chem. 270:1995;10377-10379.
11. Komiyama T., Quan L.T., Salvesen G.S. Inhibition of cysteine and serine proteinases by the cowpox virus serpin CrmA. Adv. Exp. Med. Biol. 389:1996;173-176.
12. Bode W., Huber R. Natural protein proteinase inhibitors and their interaction with proteinases. Eur. J. Biochem. 204:1992;433-451.
13. Marshall C.J. Evolutionary relationships among the serpins. Phil. Trans. R. Soc. Lond. B 342:1993;101-119.
14. 1-antitrypsin for structure and function of serpins. Biochemistry. 28:1989;8966-8971.
15. 1-proteinase inhibitor: crystal structure analysis of two modifications, molecular model and preliminary analysis of the implications for function. J. Mol. Biol. 177:1984;531-556.
16. 1-antichymotrypsin at 2.7 Å resolution and its comparison with other serpins. J. Mol. Biol. 218:1991;595-606.
17. Schreuder H., Theunissen H.et al. Crystallization and preliminary X-ray analysis of human antithrombin III. J. Mol. Biol. 229:1993;249-250.
18. Mourey L., Samama J.P., Delarue M., Petitou M., Choay J., Moras D. Crystal structure of cleaved bovine antithrombin III at 3.2 Å resolution. J. Mol. Biol. 232:1993;223-241.
19. Baumann U., Bode W., Huber R., Travis J., Potempa J. Crystal structure of cleaved equine leucocyte elastase inhibitor determined at 1.95 Å resolution. J. Mol. Biol. 226:1992;1207-1218.
20. Carrell R.W., Stein P.E., Fermi G., Wardell M.R. Biological implications of 3 Å structure of dimeric antithrombin. Structure. 2:1994;257-270.
21. Whinna H.C., Blinder M.A., Szewczyk M., Tollefsen D.M., Church F.C. Role of lysine 173 in heparin binding to heparin cofactor II. J. Biol. Chem. 266:1991;8129-8135.
22. Dickinson J.L., Norris B.J., Jensen P.H., Antalis T.M. The C-D interhelical domain of the serpin plasminogen activator inhibitor-type 2 is required for protection from TNF-alpha induced apoptosis. Cell Death Differ. 5:1998;163-171.
23. Chuang T.L., Schleef R.R. Identification of a nuclear targeting domain in the insertion between helices C and D in protease inhibitor-10. J. Biol. Chem. 274:1999;11194-11198.
24. Gettins P., Patston P.A., Schapira M. The role of conformational changes in serpin structure and function. BioEssays. 15:1993;461-467.
25. Wright H.T., Scarsdale J.N. Structural basis for serpin inhibitor activity. Proteins. 22:1995;210-225.
26. Elliott P.R., Lomas D.A., Carrell R.W., Abrahams J.P. Inhibitory conformation of the reactive loop of alpha 1-antitrypsin. Nat. Struct. Biol. 3:1996;676-681.
27. Schulze A.J., Frohnert P.W., Engh R.A., Huber R. Evidence for the extent of insertion of the active site loop of intact α1-proteinase inhibitor in β-sheet A. Biochemistry. 31:1992;7560-7565.
28. 1-Proteinase inhibitor variant T345R. Influence of P14 residue on substrate and inhibitory pathways. Biochemistry. 33:1994;8538-8547.
29. Thornberry N.A., Nicholson D.W.et al. A combinatorial approach defines specificities of members of the caspase family and granzyme B. J. Biol. Chem. 272:1997;17907-17911.
30. Ekert P.G., Silke J., Vaux D.L. Inhibition of apoptosis and clonogenic survival of cells expressing crmA variants: optimal caspase substrates are not necessarily optimal inhibitors. EMBO J. 18:1999;330-338.
31. Madison E.L., Goldsmith E.J., Gerard R.D., Gething M.J., Sambrook J.F. Serpin-resistant mutants of human tissue-type plasminogen activator. Nature. 339:1989;721-724.
32. Blanchard H., Grutter M.G.et al. The three-dimensional structure of caspase-8: an initiator enzyme in apoptosis. Structure. 7:1999;1125-1133.
33. Watt W., Koeplinger K.A., Mildner A.M., Heinrikson R.L., Tomasselli A.G., Watenpaugh K.D. The atomic-resolution structure of human caspase-8, a key activator of apoptosis. Structure. 7:1999;1135-1143.
34. Rotonda J., Becher J.W.et al. The three-dimensional structure of apopain/CPP32, a key mediator of apoptosis. Nat. Struct. Biol. 3:1996;619-625.
35. Fisher A.J., Cruz W., Zoog S.J., Schneider C.L., Friesen P.D. Crystal structure of baculovirus P35: role of a novel reactive-site loop in apoptotic caspase inhibition. EMBO J. 18:1999;2031-2039.
36. Zhou Q., Salvesen G.S.et al. Interaction of the baculovirus anti-apoptotic protein p35 with caspases: specificity, kinetics, and characterization of the caspase/p35 complex. Biochemistry. 37:1998;10757-10765.
37. Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:1997;307-326.
38. Navazza J. AMoRe: an automated package for molecular replacement. Acta Crystallogr. A. 50:1994;157-163.
39. Turk D. (1992). Weiterentwicklung eines Programmes für Molekülgraphik und Elektronendichte-Manipulation und seine Anwendung auf verschiedene Protein-Strukturaufklärungen. PhD Thesis, Technische Universität, München, Germany.
40. Brünger A.T., Warren G.L.et al. Crystallography & NMR system (CNS): a new software suite for macromolecular structure determination. Acta Crystallogr. D 54:1998;905-921.
41. Engh R.A., Huber R. Accurate bond and angle parameters for X-ray protein-structure refinement. Acta Crystallogr. A 47:1991;392-400.
42. Yeates T.O. Detecting and overcoming crystal twinning. Methods Enzymol. 276:1997;344-358.
43. Sheldrick G.M., Schneider T.R. SHELXL: high resolution refinement. Methods Enzymol. 277:1997;319-343.
44. Stennicke H.R., Salvesen G.S. Caspases: preparation and characterization. Methods. 17:1999;313-319.
45. Knight C.G. The characterization of enzyme inhibition. Barrett A.J., Salvesen G. Proteinase Inhibitors. 1986;23-51 Elsevier Science Publishers BV, Amsterdam.
46. Kraulis P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24:1991;946-950.
47. Merritt E.A., Murphy M.E.P. Raster3D Version 2.0 - a program for photorealistic molecular graphics. Acta Crystallogr. D 50:1994;869-873.
48. Barton G.J. ALSCRIPT: a tool to format multiple sequence alignments. Protein Eng. 6:1993;37-40.
49. Esnouf R.M. An extensively modified version of MolScript that includes greatly enhances coloring capabilities. J. Mol. Graph. 15:1997;132-134.