Insights into the role of oligomeric state on the biological activities of crotoxin: Crystal structure of a tetrameric phospholipase A2 formed by two isoforms of crotoxin B from Crotalus durissus terrificus venom

Proteins: Structure, Function and Genetics

Volumn 72, Issue 3, 2008, Pages 883-891

  Marchi Salvador, Daniela P ^a   Corrêa, Luiz C ^a   Magro, Angelo J ^a   Oliveira, Clayton Z ^b   Soares, Andreimar M ^b   Fontes, Marcos R M ^a  

^a SÃO PAULO STATE UNIVERSITY UNESP   (Brazil)

^b UNIVERSITY OF SÃO PAULO   (Brazil)

Author keywords

Asp49 phospholipase A2; Crotalus durissus terrificus venom; Crotoxin B; Crystal structure; Neurotoxic activity; Oligomerization

Indexed keywords

CANNABINOID 1 RECEPTOR; CANNABINOID 2 RECEPTOR; CROTOXIN; CROTOXIN B; DIMER; GLUTAMINE; OLIGOMER; PHOSPHOLIPASE A2; SERINE; SNAKE VENOM; TETRAMER;

ARTICLE; BINDING AFFINITY; BINDING SITE; BIOLOGICAL ACTIVITY; CONFORMATION; CRYSTAL STRUCTURE; NEUROTOXICITY; NONHUMAN; OLIGOMERIZATION; PRESYNAPTIC MEMBRANE; PRIORITY JOURNAL; PROTEIN ASSEMBLY;

AMINO ACID SEQUENCE; ANIMALS; CROTALUS; CROTOXIN; CRYSTALLOGRAPHY, X-RAY; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ISOENZYMES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PHOSPHOLIPASES A2; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; SEQUENCE ALIGNMENT;

CROTALUS DURISSUS TERRIFICUS;

EID: 47349114449     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21980     Document Type: Article

References (48)

1. 2 superfamily and its group numbering system. Biochim Biophys Acta 2006;1761:1246-1259.
2. 2 enzymes: structure, function and mechanism. Chichester: Wiley; 1997. pp 321-352.
3. Ownby CL. Structure, function and biophysical aspects of the myotoxins from snake venoms. J Toxicol Toxin Rev 1998;17:1003-1009.
4. 2? Biochimie 2000;82:815-831.
5. Slotta KH, Fraenkel-Conrat HL. Schlangengifte. III. Mitteilung: Reinigung und Kristallisation des Klapperschlangengiftes. Ber Dtsch Chem Ges B 1938;71:1076-1081.
6. 2 neurotoxin from the South American rattlesnake Crotalus durissus terrificus: purification of several isoforms and comparison of their molecular structure and of their biological activities. Biochemistry 1988;27:730-738.
7. 2 complex. Toxicon 1984;22:85-98.
8. 2 enzymes: structure, function and mechanism. Chichester: Wiley; 1997. pp 269-285.
9. Monteiro HSA, da Silva IMSC, Martins AMC, Fonteies MC. Effects of Crotalus durissus terrificus venom and crotoxin on the isolated rat kidney. Braz J Med Biol Res 2001;34:1347-1352.
10. Hendon RA, Fraenkel-Conrat H. Biological role of the two components of Cro. Proc Natl Acad Sci USA 1971;68:1560-1563.
11. Corin RE, Viskatis LJ, Vidal JC, Etcheverry MA. Cytotoxicity of Cro on murine erythroleukemia cells in vitro. Invest New Drugs 1993;11:11-15.
12. Rudd CJ, Viskatis LJ, Vidal JC, Etcheverry MA. In vitro comparison of cytotoxic effects of Cro against three human tumors and normal human epidermal keratinocyte cell line. Invest New Drugs 1994;12:183-184.
13. 2. NSC-624244) in patient with advanced cance. Clin Cancer Res 2002;8:1033-1041.
14. Zhang HL, Han R, Chen ZX, Chen BW, Gu ZL, Reid PF, Raymond LN, Qin ZH. Opiate and acetylcholine-independent analgesic actions of crotoxin isolated from Crotalus durissus terrificus venom. Toxicon 2006;48:175-182.
15. Faure G, Bon C. Several isoforms of crotoxin are present in individual venoms from the South American rattlesnake Crotalus durissus terrificus. Toxicon 1987;25:229-234.
16. Faure G, Choumet V, Bouchier C, Camoin L, Guillaume JL, Monegier B, Vuilhorgne M, Bon C. The origin of the diversity of crotoxin isoforms in the venom of Crotalus durissus terrificus. Eur J Biochem 1994;223:161-164.
17. Soares AM, Rodrigues VM, Homsi-Brandeburgo MI, Toyama MH, Lombardi FR, Arni RK, Giglio JR. A rapid procedure for the isolation of the Lys-49 myotoxin II from Bothrops moojeni (caissaca) venom: biochemical characterization, crystallization, myotoxic and edematogenic activities. Toxicon 1998;36:503-514.
18. 2 subunit of crotoxin from Crotalus durissus terrificus snake venom, on its enzymatic and pharmacological activities. Int J Biochem Cell Biol 2001;33:877-888.
19. LaemmLi UK. Cleavage of stuctural proteins during the assembly of the head of bacteriophage T4. Nature 1970;227:680-685.
20. Jancarik J, Kim SH. Sparse matrix sampling: a screening method for crystallization of proteins. J Appl Cryst 1991;24:409-411.
21. Ducruix A, Giegé R. Crystallization of nucleic acids and proteins (a practical approach). New York: Oxford University Press; 1992. 464 p.
22. 2 formed by two isoforms of crotoxin B from Crotalus durissus terrificus venom. Acta Crystallogr F 2007;63:1067-1069.
23. Otwinowski Z, Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 1997;276:307-326.
24. Brünger AT, Adams PD, Clore GM, DeLano WL, Gros P, Grosse-Kunstleve RW, Jiang JS, Kuszewski J, Nilges M, Pannu NS, Read RJ, Rice LM, Simonson T, Warren GL. Crystallography and NMR system (CNS): a new software system for macromolecular structure determination. Acta Crystallogr D 1998;54:905-921.
25. Navaza J. AMoRe: an automated package for molecular replacement. Acta Crystallogr. A 1994;50:157-163.
26. 2 homologue. Proteins: Struct Funct Genet 1998;30:442-454.
27. Jones TA, Bergdoll M, Kjeldgaard M. O: a macromolecule modeling environment. In: Bugg CE, Ealick SE, editors. Crystallographic and modeling methods in molecular design. New York: Springer-Verlag; 1990. pp 189-195.
28. Laskowski RA, MacArthur MW, Moss DS, Thornton JM. PROCHECK: a program to check the stereochemical quality of protein structures. J Appl Crystallogr 1993;26:283-291.
29. Krissinel E, Henrick K. Inference of macromolecular assemblies from crystalline state. J Mol Biol 2007;372:774-797.
30. DeLano WL. The PyMOL molecular graphics system. San Carlos, CA: Delano Scientific LLC; 2002. Available at http://www.pymol.org.
31. Ramachandran GN, Sasisekharan V. Conformation of polypeptides and proteins. Adv Protein Chem 1968;23:283-438.
32. 2 from bovine pancreas and Crotalus atrox venom. J Biol Chem 1985;260:11627-11636.
33. Nicholas KB, Nicholas HB, Jr, Deerfield DW, II. GeneDoc: analysis and visualization of genetic variation. EMBNETNEWS 1997;4:1-4.
34. 2 enzymes: structure, function and mechanism. Chichester: Wiley; 1997. pp 321-352.
35. Steiner RA, Rozeboom HJ, de Vries A, Kalk KH, Murshudov GN, Wilson KS, Dijkstra BW. X-ray structure of bovine pancreatic phospholipase A2 at atomic resolution. Acta Crystallogr D 2001;57:516-526.
36. 2 from Indian saw-scaled viper (Echis carinatus) at 2.6 Å resolution reveals a novel intermolecular interaction. Acta Crystallogr D 2004;60:66-72.
37. 2: relationship to interface binding. Biochemistry 2001;40:609-617.
38. 2 by two-photon excitation fluorescence correlation spectroscopy. Biochemistry 2001;40:6903-6911.
39. 2 and α-tocopherol at 1.8 Å resolution. J Mol Biol 2002;320:215-222.
40. 2 in the monomeric and dimeric states: insights into its oligomeric state. Biochem Biophys Res Commun 2004;323:24-31.
41. Magro AJ, Takeda AAS, Soares AM, Fontes MRM. Structure of BthA-I complexed with p-bromophenacyl bromide: possible correlations with lack of pharmacological activity. Acta Crystallogr D 2005;61:1670-1677.
42. 2 at 1.6 Å resolution. Proteins: Struct Funct Bioinform 2005;59:856-863.
43. Tang L, Zhou YC, Lin ZJ. Structure of agkistrodotoxin in an orthorhombic crystal form with six molecules per asymmetric unit. Acta Crystallogr D 1999;55:1986-1996.
44. 2 enzymes. Toxicon 2003;42:827-840.
45. Krizaj I, Turk D, Ritonja A, Gubensek F. Primary structure of ammodytoxin C further reveals the toxic site of ammodytoxin. Biochim Biophys Acta 1989;999:198-202.
46. 2. Toxicon 1998;36:75-92.
47. 2 by sequence analysis and site directed mutagenesis. Toxicon 2003;42:869-883.
48. Rouault M, Rash LD, Escoubas P, Boilard E, Bollinger J, Lomonte B, Maurin T, Guillaume C, Canaan S, Deregnaucourt C, Schrével J, Doglio A, Gutiérrez JM, Lazdunski M, Gelb MH, Kumar S, Tamura K, Jakobsen IB, Nei M. MEGA2: molecular evolutionary genetics analysis software. Bioinformatics 2001;17:1244-1245.