메뉴 건너뛰기




Volumn 333, Issue 2, 2003, Pages 367-376

Crystal structures of the free and anisic acid bound triple mutant of phospholipase A2

Author keywords

Anisic acid; Crystal structure; Phospholipase A2; Surface loop; Triple mutant

Indexed keywords

ANISIC ACID; CALCIUM ION; CARBOXYLIC ACID; HEXYLENE GLYCOL; OXYGEN; PHENOL; PHOSPHOLIPASE A2; TYROSINE; WATER;

EID: 0141706625     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2003.08.032     Document Type: Article
Times cited : (28)

References (44)
  • 9
    • 0036714237 scopus 로고    scopus 로고
    • 2 inhibition for the synthesis of prostaglandins by the plant alkaloid aristolochic acid from a 1.7 Å crystal structure
    • 2 inhibition for the synthesis of prostaglandins by the plant alkaloid aristolochic acid from a 1.7 Å crystal structure. Biochemistry. 41:2002;10914-10919.
    • (2002) Biochemistry , vol.41 , pp. 10914-10919
    • Chandra, V.1    Jasti, J.2    Kaur, P.3    Betzel, C.4    Srinivasan, A.5    Singh, T.P.6
  • 12
    • 0034256915 scopus 로고    scopus 로고
    • Molecular mechanism of lung hemorrhage induction by VRV-PL-VIIIa from Russell's viper (Vipera russelli) venom
    • Uma B., Gowda T.V. Molecular mechanism of lung hemorrhage induction by VRV-PL-VIIIa from Russell's viper (Vipera russelli) venom. Toxicon. 38:2000;1129-1147.
    • (2000) Toxicon , vol.38 , pp. 1129-1147
    • Uma, B.1    Gowda, T.V.2
  • 17
    • 0025073785 scopus 로고
    • 2 engineering. 3. Replacement of lysine-56 by neutral residues improves catalytic efficiency significantly, alters substrate specificity, and clarifies the mechanism of interfacial recognition
    • 2 engineering. 3. Replacement of lysine-56 by neutral residues improves catalytic efficiency significantly, alters substrate specificity, and clarifies the mechanism of interfacial recognition. J. Am. Chem. Soc. 112:1990;3704-3706.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 3704-3706
    • Noel, J.P.1    Deng, T.2    Hamilton, K.J.3    Tsai, M.-D.4
  • 20
    • 0028978839 scopus 로고
    • 2 engineering. Probing the structural and functional roles of N-terminal residues with site-directed mutagenesis, X-ray, and NMR
    • 2 engineering. Probing the structural and functional roles of N-terminal residues with site-directed mutagenesis, X-ray, and NMR. Biochemistry. 34:1995;7322-7334.
    • (1995) Biochemistry , vol.34 , pp. 7322-7334
    • Liu, X.H.1    Zhu, H.X.2    Huang, B.H.3    Rodgers, J.4    Yu, B.-Z.5    Kumar, A.6
  • 24
  • 31
    • 0028588046 scopus 로고
    • Structure and function of the catalytic site mutant Asp 99 Asn of phospholipase A2: Absence of the conserved structural water
    • Kumar A., Sekharudu C., Ramakrishnan B., Dupureur C.M., Zhu H., Tsai M.-D., Sundaralingam M. Structure and function of the catalytic site mutant Asp 99 Asn of phospholipase A2: absence of the conserved structural water. Protein Sci. 3:1994;2082-2088.
    • (1994) Protein Sci. , vol.3 , pp. 2082-2088
    • Kumar, A.1    Sekharudu, C.2    Ramakrishnan, B.3    Dupureur, C.M.4    Zhu, H.5    Tsai, M.-D.6    Sundaralingam, M.7
  • 32
    • 0030615005 scopus 로고    scopus 로고
    • 2 engineering. Structural and functional roles of the highly conserved active site residue aspartate-99
    • 2 engineering. Structural and functional roles of the highly conserved active site residue aspartate-99. Biochemistry. 36:1997;3101-3114.
    • (1997) Biochemistry , vol.36 , pp. 3101-3114
    • Sekar, K.1    Yu, B.-Z.2    Rogers, J.3    Lutton, J.4    Liu, X.5    Chen, X.6
  • 34
    • 0029661921 scopus 로고    scopus 로고
    • 2 engineering. Deletion of the C-terminus segment changes substrate specificity and uncouples calcium and substrate binding at the zwitterionic interface
    • 2 engineering. Deletion of the C-terminus segment changes substrate specificity and uncouples calcium and substrate binding at the zwitterionic interface. Biochemistry. 36:1996;12164-12174.
    • (1996) Biochemistry , vol.36 , pp. 12164-12174
    • Huang, B.1    Yu, B.-Z.2    Rogers, J.3    Byeon, I.J.4    Sekar, K.5    Chen, X.6
  • 38
    • 0026597444 scopus 로고
    • Free R-value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brunger A.T. Free R-value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature. 355:1992;472-474.
    • (1992) Nature , vol.355 , pp. 472-474
    • Brunger, A.T.1
  • 41
    • 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. 276:1997;307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 42
    • 0022333120 scopus 로고
    • Diffraction methods for biological macromolecules. Interactive computer graphics: FRODO
    • Jones T.A. Diffraction methods for biological macromolecules. Interactive computer graphics: FRODO. Methods Enzymol. 115:1985;157-171.
    • (1985) Methods Enzymol. , vol.115 , pp. 157-171
    • Jones, T.A.1
  • 44
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24:1991;946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.