Crystal structures of the complexes of a group IIA phospholipase A 2 with two natural anti-inflammatory agents, anisic acid, and atropine reveal a similar mode of binding

Proteins: Structure, Function and Genetics

Volumn 64, Issue 1, 2006, Pages 89-100

  Singh, Nagendra ^a   Jabeen, Talat ^a   Pal, Aritra ^a   Sharma, Sujata ^a   Perbandt, Markus ^b   Betzel, Christian ^b   Singh, Tej P ^a  

^a ALL INDIA INSTITUTE OF MEDICAL SCIENCES   (India)

^b DESY   (Germany)

Author keywords

Activity; Affinity; Anti inflammatory compounds; Binding constant; Complex; Plant alkaloid; X ray intensity data

Indexed keywords

ALKALOID; ANISIC ACID; ANTIINFLAMMATORY AGENT; ARACHIDIC ACID; ARACHIDONIC ACID; ARISTOLOCHIC ACID; ASPARTIC ACID; ATROPINE; HISTIDINE; PHOSPHOLIPASE A2; SNAKE VENOM;

ACCURACY; ARTICLE; BINDING SITE; COMPLEX FORMATION; CRYSTAL STRUCTURE; CRYSTALLIZATION; DRUG PROTEIN BINDING; ENZYME INHIBITION; ENZYME ISOLATION; ENZYME PURIFICATION; ENZYME SUBSTRATE COMPLEX; HYDROGEN BOND; HYDROPHOBICITY; MOLECULAR INTERACTION; MOLECULAR SIZE; MOLECULAR WEIGHT; PRIORITY JOURNAL; PROTEIN CONFORMATION; X RAY CRYSTALLOGRAPHY;

ANIMALS; ANTI-INFLAMMATORY AGENTS; ATROPINE; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; KINETICS; PHOSPHOLIPASES A; VIPER VENOMS; VIPERIDAE;

BOS TAURUS; DABOIA RUSSELLII PULCHELLA;

EID: 33744801380     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1080/00150190500327165     Document Type: Article

References (45)

1. 2. Biochem Biophys Acta 1993;1170: 217-231.
2. 2 superfamily of signal transduction enzymes. Trends Biol Sci 1997;1:1-2.
3. 2. J Biol Chem 1994;269:13057-13060.
4. 2. Annu Rev Biochem 1995;64:653-688.
5. 2: relationship to interface binding. Biochemistry 2001;40:609-617.
6. 2 from the anion-assisted dimer structure. Biochemistry 2001;40: 11411-11422.
7. 2 (IIa) with antiinflammatory activity. Chembiochem 2003;4:181-185.
8. 2 in a complex with a transition state analogue. Science 1990;250:1563-1566.
9. 2 with the inhibitor 1-hexadecyl-3-(trifluoroethyl)-sn-glycero-2-phosphomethanol. Biochemistry 1997;36:14186-14191.
10. 2 complexed with a substrate-derived inhibitor. Nature 1990;347:689-691.
11. 2: X-ray structure of the complex and interfacial selection of inhibitors from a structural library. Bioorg Med Chem Lett 1999;9:1097-1102.
12. 2, alters human neutrophil arachidonic acid release and metabolism and prolongs survival in murine endotoxin shock. J Pharmacol Exp Ther 1995;274:1254-1262.
13. 2 inhibition for the synthesis of prostaglandins by the plant alkaloid aristolochic acid from a 1.7 Å crystal structure. Biochemistry 2002;41:10914-10919.
14. 2 from berries of Schinus terebinthifolius. Phytochemistry 1995;39:537-547.
15. 2 with antiinflammatory activity. J Med Chem 1993;36:3029-3031.
16. 2 by the antiinflammatory agent BMS-181162. J Biol Chem 1995;270:274-280.
17. 2 inhibitors from ascomycetes. J Antibiot (Tokyo) 1991;44:1467-1470.
18. 2 specific inhibitor from ascomycetes. J Antibiot (Tokyo) 1994;47: 631-638.
19. 2. J Am Chem Soc 1994;116:759-760.
20. Hite GA, Mihelich ED, Tulio S, Edmund WS. Eur Pat 0 846 687 A1 (1998).
21. 2 and a designed peptide Leu-Ala-Ile-Tyr-Ser (LAIYS). Acta Crystallogr 2002;D58:1813-1819.
22. 2 and a potent peptide inhibitor Phe-Leu-Ser-Tyr-Lys at 1.8 Å resolution. J Biol Chem 2002;277:41079-41085.
23. 2 from Naja naja sagittifera (group I) and a designed peptide inhibitor Val-Ala-Phe-Arg-Ser (VAFRS) at 1.9 Å resolution reveals unique features. Biochemistry 2003;42:11701-11706.
24. 2 and alpha-tocopherol at 1.8 Å resolution. J Mol Biol 2002;320:215-222.
25. 2. Nat Struct Biol 1995;2:458-465.
26. 2 modified by p-bromo-phenacyl-bromide. Toxicon 1998;36:875-886.
27. 2 in a complex with a transition-state analog. Science 1990;250:1560-1563.
28. 2-elaidoylamide complex: a new mode of inhibition. Biochem Biophys Res Commun 2004;319:1314-1321.
29. 2 from Agkistrodon halys blomhoffii venom to micelles of n-hexadecylphosphorylcholine. J Biochem (Tokyo) 1984;96:1427-1436.
30. Szabo A, Stolz L, Granzow R. Surface plasmon resonance and its use in biomolecular interaction analysis (BIA). Curr Opin Struct Biol 1995;5:699-705.
31. Nieba L, Krebber A, Plückhun A. Competition BIAcore for measuring true affinities: large differences from values determined from binding kinetics. Anal Biochem 1996;234:155-165.
32. Otwinowski Z, Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 1997;276:307-325.
33. Navaza J. AMoRe: an automated package for molecular replacement. Acta Crystallogr A 1994;50:157-163.
34. 2) at 1.9 Å resolution. Acta Crystallogr D 2001;57:1793-1797.
35. Murshudov GN, Vagin AA, Dodson EJ. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr D 1997;53:240-255.
36. Collaborative Computational Project, Number 4. The CCP4 suite-programs for protein crystallography. Acta Crystallogr D 1994;50: 760-763.
37. Jones TA, Zou J, Cowan SW, Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr A 1991;47:110-119.
38. Laskowski R, Macarthur M, Moss D, Thornton J. PROCHECK: a program to check the stereochemical quality of protein structures. J Appl Crystallogr 1993;26:283-290.
39. Vaguine AA, Richelle J, Wodak SJ. SFCHECK: a unified set of procedures for evaluating the quality of macromolecular structure-factor data and their agreement with the atomic model. Acta Crystallogr D 1999;55:191-205.
40. Ramachandran GN, Sasisekharan V. Conformation of polypeptides and proteins. Adv Prot Chem 1968;23:283-438.
41. 2-type presynaptic neurotoxin from agkistrodon halys pallas. J Mol Biol 1998;282:1-11.
42. Colapietro M, Domenicano A. Structural studies of benzene derivatives. IV. Refinement of the crystal structure of p-methoxybenzoic acid. Acta Crystallogr 1978;B34:277-3280.
43. 2. J Mol Biol 2003;333:367-376.
44. 2 and aspirin at 1.9 Å resolution. J Drug Target 2005;2:113-119.
45. Nicholls A, Sharp KA, Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 1991;11:281-296.