Crystallization and preliminary X-ray diffraction analysis of an acidic phospholipase A2 complexed with p-bromophenacyl bromide and α-tocopherol inhibitors at 1.9- and 1.45-Å resolution

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1699, Issue 1-2, 2004, Pages 281-284

  Takeda, Agnes A S ^a   Dos Santos, Juliana I ^a   Marcussi, Silvana ^b   Silveira, Lucas B ^b   Soares, Andreimar M ^b   Fontes, Marcos R M ^a  

^a SÃO PAULO STATE UNIVERSITY UNESP   (Brazil)

^b UNIVERSITY OF RIBEIRÃO PRETO   (Brazil)

Author keywords

Tocopherol; Acidic phospholipase A2; Bothrops jararacussu venom; BthA I PLA2; Crystallization; p Bromophenacyl bromide; phospholipase A2; PLA 2; X ray crystallography

Indexed keywords

4 BROMOPHENACYL BROMIDE; ALPHA TOCOPHEROL; BATROXOBIN; PHOSPHOLIPASE A2; PHOSPHOLIPASE A2 INHIBITOR; SNAKE VENOM;

ARTICLE; COMPLEX FORMATION; CRYSTALLIZATION; DRUG PROTEIN BINDING; ENZYME ANALYSIS; ENZYME ISOLATION; ENZYME STRUCTURE; PRIORITY JOURNAL; PROTEIN QUATERNARY STRUCTURE; SNAKE; STRUCTURE ANALYSIS; X RAY DIFFRACTION;

ACETOPHENONES; ANIMALS; ANTIOXIDANTS; BINDING SITES; BOTHROPS; CROTALID VENOMS; CRYSTALLIZATION; ENZYME INHIBITORS; PHOSPHOLIPASES A; VITAMIN E; X-RAY DIFFRACTION;

BOTHROPS; BOTHROPS JARARACUSSU; SERPENTES;

EID: 2542458406     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2004.02.005     Document Type: Article

References (34)

1. 2 enzymes: classification and characterization. Biochim. Biophys. Acta. 1488:2000;1-19
2. Rosenberg P. Shier W., Mebs D. Handbook of Toxinology. 1990;67-277 Marcel Dekker, New York
3. 2 Enzymes: Structure, Function and Mechanism. 1997;321-352 Wiley, Chichester
4. Ownby C.L. Structure, function and byophysical aspects of the myotoxins from snake venoms. J. Toxicol., Toxin Rev. 17:1998;1003-1009
5. 2? Biochimie. 82:2000;815-831
6. 2. Toxicon. 27:1989;613-635
7. 2 from snake venoms: Effects on catalytic and pharmacological properties. Review. Toxicon. 42:2004;855-868
8. Needleman P., Turk J., Jakschik B.A., Morrison A.R., Lefkowith J.B. Arachidonic acid metabolism. Annu. Rev. Biochem. 55:1986;69-102
9. Pentland A.P., Morrison A.R., Jacobs S.C., Hruza L.L., Hebert J.S., Packer L. Tocopherol analogs suppress arachidonic acid metabolism via phospholipase inhibition. J. Biol. Chem. 267:1992;1603-1608
10. Abate A., Yang G., Dennery P.A., Oberle S., Schroder H. Synergistic inhibition of cyclooxygenase-2 by vitamin E and aspirin. Free Radic. Biol. Med. 29:2000;1135-1142
11. Ebadi M., Srinivasan S.K., Baxi M.D. Oxidative stress and antioxidant therapy in Parkinson's disease. Prog. Neurobiol. 48:1996;1-19
12. Sano M., Ernesto C., Thomas R.G., Klauber M.R., Schafer K., Grundman M., et al. A controlled trial of selegiline, alpha-tocopherol, or both as treatment for Alzheimer's disease. The Alzheimer's Disease Cooperative Study. N. Engl. J. Med. 336:1997;1216-1222
13. 2 and alpha-tocopherol at 1.8 A resolution. J. Mol. Biol. 320:2002;215-222
14. Rodrigues V.M., Soares A.M., Mancin A.C., Fontes M.R.M., Homsi-Brandeburgo M.I., Giglio J.R. Geographic variations in the composition of myotoxins from Bothrops neuwiedi snake venom: biochemical characterization and biological activity. Comp. Biochem. Physiol. 121A:1998;215-222
15. 2 homologue from Bothrops neuwiedi venom. Arch. Biochem. Biophys. 378:2000;210-219
16. 2 modified by p-bromo-phenacyl-bromide. Toxicon. 36:1998;875-886
17. 2 covalently inhibited by p-bromo-phenacyl-bromide. J. Biol. Chem. 200:1988;181-188
18. Arni R.K., Ward R.J., Gutiérrez J.M., Tulinsky A. Structure of a calcium-independent phospholipase-like myotoxic protein from Bothrops asper. Acta Crystallogr., D Biol. Crystallogr. 51:1995;311-317
19. 2 homologue from Bothrops moojeni venom. Prot. Peptide Letters. 4:1997;329-334
20. 2 homologue. Protein Struct.-Funct. Gen. 30:1998;442-454
21. 2 - A hypothesis: the crystal structure of piratoxin II complexed to fatty acid. Biochemistry. 40:2001;28-36
22. 2: quaternary structure and inhibition mechanism insights. Biochem. Biophys. Res. Commun. 311:2003;713-720
23. 2 from Bothrops lanceolatus (fer de lance) venom: molecular and enzymatic properties. Toxicon. 32:1994;1069-1081
24. 2 from Bothrops neuwiedii venom. Arch. Biochem. Biophys. 318:1995;65-70
25. 2, from the venom of the snake Bothrops jararaca: purification, primary structure analysis, and its characterization as a platelet-aggregation-inhibiting factor. Arch. Biochem. Biophys. 367:1999;26-32
26. Homsi-Brandeburgo M.I., Queiroz L.S., Santo-Neto H., Rodrigues-Simioni L., Giglio J.R. Fractionation of Bothrops jararacussu snake venom: partial chemical characterization and biological activity of bothropstoxin. Toxicon. 26:1988;615-627
27. 2 activity. J. Protein Chem. 17:1998;381-386
28. 2 from Bothrops jararacussu snake venom. Biochem. Pharmacol. 64:2002;723-732
29. 2 from Bothrops jararacussu venomous gland library. Protein Expr. Purif. 2004;. (in press)
30. 2 cDNA from Bothrops jararacussu venomous gland. Protein Expr. Purif. 2003;. (submitted for publication)
31. Jancarik J., Kim S.H. Sparce matrix sampling: a screen method for crystallization of proteins. J. Appl. Crystallogr. 24:1991;409-411
32. MacPherson A. Preparation and Analysis of Protein Crystals. 1982;Wiley, New York
33. Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:1997;307-326
34. Navaza J. AMoRe: an automated package for molecular replacement. Acta Crystallogr. A50:1994;157-163