메뉴 건너뛰기




Volumn 62, Issue 2, 2006, Pages 329-337

Crystal structure of a heterodimer of phospholipase A2 from Naja naja sagittifera at 2.3 Å resolution reveals the presence of a new PLA 2-like protein with a novel Cys 32-Cys 49 disulphide bridge with a bound sugar at the substrate-binding site

Author keywords

Crystal structure; Cys PLA2; Heterodimer; PLA2; Sequence determination; X ray diffraction

Indexed keywords

CARBOHYDRATE; COORDINATION COMPOUND; CYSTEINE; DIMER; MONOMER; N ACETYLGLUCOSAMINE; PHOSPHOLIPASE A2; PHOSPHOLIPASE A2 LIKE PROTEIN; SNAKE VENOM; SOLVENT; UNCLASSIFIED DRUG; ZINC ION;

EID: 30144443653     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.20708     Document Type: Article
Times cited : (13)

References (38)
  • 1
    • 0021105553 scopus 로고
    • Classification of phospholipases A2 according to sequence. Evolutionary and pharmacological implications
    • Dufton MJ, Hider RC. Classification of phospholipases A2 according to sequence. Evolutionary and pharmacological implications. Eur J Biochem 1983;137:545-551.
    • (1983) Eur J Biochem , vol.137 , pp. 545-551
    • Dufton, M.J.1    Hider, R.C.2
  • 6
    • 0017123563 scopus 로고
    • 2 with anticoagulant activity. Isolation from Vipera berus venom and properties
    • 2 with anticoagulant activity. Isolation from Vipera berus venom and properties. Biochim Biophys Acta 1976;429:828-838.
    • (1976) Biochim Biophys Acta , vol.429 , pp. 828-838
    • Boffa, G.A.1    Boffa, M.C.2    Winchenne, J.J.3
  • 7
    • 0028982743 scopus 로고
    • Structure of beta 2-bungarotoxin: Potassium channel binding by Kunitz modules and targeted phospholipase action
    • Kwong PD, McDonald NQ, Sigler PB, Hendrickson WA. Structure of beta 2-bungarotoxin: potassium channel binding by Kunitz modules and targeted phospholipase action. Structure 1995;3: 1109-1119.
    • (1995) Structure , vol.3 , pp. 1109-1119
    • Kwong, P.D.1    McDonald, N.Q.2    Sigler, P.B.3    Hendrickson, W.A.4
  • 9
    • 0032508651 scopus 로고    scopus 로고
    • 2-type presynaptic neurotoxin from agkistrodon halys pallas
    • 2-type presynaptic neurotoxin from agkistrodon halys pallas. J Mol Biol 1998;282:1-11.
    • (1998) J Mol Biol , vol.282 , pp. 1-11
    • Tang, L.1    Zhou, Y.C.2    Lin, Z.J.3
  • 10
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski P, Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal Biochem 1987;162:156-159.
    • (1987) Anal Biochem , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 11
    • 0021364597 scopus 로고
    • Sensitive quantitative analysis of disulfide bonds in polypeptides and proteins
    • Thannhauser TW, Konishi Y, Scheraga HA. Sensitive quantitative analysis of disulfide bonds in polypeptides and proteins. Anal Biochem 1984;138:181-188.
    • (1984) Anal Biochem , vol.138 , pp. 181-188
    • Thannhauser, T.W.1    Konishi, Y.2    Scheraga, H.A.3
  • 12
    • 0021917749 scopus 로고
    • Estimation of disulfide bonds using 2-nitro-5-thiosulfobenzoic acid: Limitations
    • Damodaran S. Estimation of disulfide bonds using 2-nitro-5- thiosulfobenzoic acid: limitations. Anal Biochem 1985;145:200-204.
    • (1985) Anal Biochem , vol.145 , pp. 200-204
    • Damodaran, S.1
  • 15
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 1997;176:307-326.
    • (1997) Methods Enzymol , vol.176 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 16
    • 84920325457 scopus 로고
    • AmoRe: An automated package for molecular replacement
    • Navaza J. AmoRe: an automated package for molecular replacement. Acta Cryst A 1994;50:157-163.
    • (1994) Acta Cryst A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 19
    • 0026597444 scopus 로고
    • The free R-value: A novel statistical quantity for accessing the accuracy of crystal structures
    • Brunger AT. The free R-value: a novel statistical quantity for accessing the accuracy of crystal structures. Nature 1992;355:472-474.
    • (1992) Nature , vol.355 , pp. 472-474
    • Brunger, A.T.1
  • 20
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones TA, Zou JY, Cowan SW, Kjeldgaard. 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.
    • (1991) Acta Crystallogr A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard4
  • 22
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex N, Peitsch, MC. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 1997;18:2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 24
    • 0035815112 scopus 로고    scopus 로고
    • 2 from common krait (Bungarus caeruleus) at 2.4 a resolution: Identification and characterization of its pharmacological sites
    • 2 from common krait (Bungarus caeruleus) at 2.4 A resolution: identification and characterization of its pharmacological sites. J Mol Biol 2001;307:1049-1059.
    • (2001) J Mol Biol , vol.307 , pp. 1049-1059
    • Singh, G.1    Gourinath, S.2    Sharma, S.3    Paramasivam, M.4    Srinivasan, A.5    Singh, T.P.6
  • 27
    • 0017132404 scopus 로고
    • Action on phosphatidylcholine of the toxic phospholipase A2 from the venom of bulgarian viper (Vipera ammodytes ammodytes)
    • Aleksiev B, Tchorbanov B. Action on phosphatidylcholine of the toxic phospholipase A2 from the venom of bulgarian viper (Vipera ammodytes ammodytes). Toxicon 1976;14:477-485.
    • (1976) Toxicon , vol.14 , pp. 477-485
    • Aleksiev, B.1    Tchorbanov, B.2
  • 29
    • 0000243829 scopus 로고
    • PROCHECK: A program to check stereo-chemical quality of protein structures
    • Laskowski R, Macarthur M, Moss D, Thornton J. PROCHECK: a program to check stereo-chemical quality of protein structures. J Appl Crystallogr 1993;26:283-290.
    • (1993) J Appl Crystallogr , vol.26 , pp. 283-290
    • Laskowski, R.1    Macarthur, M.2    Moss, D.3    Thornton, J.4
  • 33
    • 0026342821 scopus 로고
    • Structures of free and inhibited human secretory phospholipase A2 from inflammatory exudate
    • Scott DL, White SP, Browning JL, Rosa JJ, Gelb MH, Sigler PB. Structures of free and inhibited human secretory phospholipase A2 from inflammatory exudate. Science 1991;254:1007-1010.
    • (1991) Science , vol.254 , pp. 1007-1010
    • Scott, D.L.1    White, S.P.2    Browning, J.L.3    Rosa, J.J.4    Gelb, M.H.5    Sigler, P.B.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.