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Volumn 445, Issue 7126, 2007, Pages 447-451

The APOBEC-2 crystal structure and functional implications for the deaminase AID

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION INDUCED CYTIDINE DEAMINASE; APOLIPOPROTEIN B MESSENGER RNA EDITING ENZYME CATALYTIC POLYPEPTIDE 2; DEAMINASE; POLYPEPTIDE; TETRAMER; UNCLASSIFIED DRUG;

EID: 33846555779     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature05492     Document Type: Article
Times cited : (182)

References (28)
  • 1
    • 14344260225 scopus 로고    scopus 로고
    • Reward versus risk: DNA cytidine deaminases triggering immunity and disease
    • Pham, P., Bransteitter, R. & Goodman, M. F. Reward versus risk: DNA cytidine deaminases triggering immunity and disease. Biochemistry 44, 2703-2715 (2005).
    • (2005) Biochemistry , vol.44 , pp. 2703-2715
    • Pham, P.1    Bransteitter, R.2    Goodman, M.F.3
  • 2
  • 3
    • 33745222090 scopus 로고    scopus 로고
    • Bransteitter, R., Sneeden, J. L., Allen, S., Pham, P. & Goodman, O. M. F. First AID (activation-induced cytidine deaminase) is needed to produce high affinity isotype-switched antibodies. J. Biol. Chem. 281, 16833-16836 (2006).
    • Bransteitter, R., Sneeden, J. L., Allen, S., Pham, P. & Goodman, O. M. F. First AID (activation-induced cytidine deaminase) is needed to produce high affinity isotype-switched antibodies. J. Biol. Chem. 281, 16833-16836 (2006).
  • 4
    • 33744931693 scopus 로고    scopus 로고
    • Multifaceted antiviral actions of APOBEC3 cytidine deaminases
    • Chiu, Y. L. & Greene, W. C. Multifaceted antiviral actions of APOBEC3 cytidine deaminases. Trends Immunol. 27, 291-297 (2006).
    • (2006) Trends Immunol , vol.27 , pp. 291-297
    • Chiu, Y.L.1    Greene, W.C.2
  • 5
    • 31144469701 scopus 로고    scopus 로고
    • Role and mechanism of action of the APOBEC3 family of antiretroviral resistance factors
    • Cullen, B. R. Role and mechanism of action of the APOBEC3 family of antiretroviral resistance factors. J. Virol. 80, 1067-1076 (2006).
    • (2006) J. Virol , vol.80 , pp. 1067-1076
    • Cullen, B.R.1
  • 6
    • 33646468134 scopus 로고    scopus 로고
    • APOBEC deaminases as cellular antiviral factors: A novel natural host defense mechanism
    • Franca, R., Spadari, S. & Maga, G. APOBEC deaminases as cellular antiviral factors: a novel natural host defense mechanism. Med. Sci. Monit. 12, RA92-RA98 (2006).
    • (2006) Med. Sci. Monit , vol.12
    • Franca, R.1    Spadari, S.2    Maga, G.3
  • 7
    • 33745541663 scopus 로고    scopus 로고
    • Interferon-inducible expression of APOBEC3 editing enzymes in human hepatocytes and inhibition of hepatitis B virus replication
    • Bonvin, M. et al. Interferon-inducible expression of APOBEC3 editing enzymes in human hepatocytes and inhibition of hepatitis B virus replication. Hepatology 43, 1364-1374 (2006).
    • (2006) Hepatology , vol.43 , pp. 1364-1374
    • Bonvin, M.1
  • 8
    • 0037176913 scopus 로고    scopus 로고
    • Crystal structure of the tetrameric cytidine deaminase from Bacillus subtilis at 2.0 Å resolution
    • Johansson, E., Mejlhede, N., Neuhard, J. & Larsen, S. Crystal structure of the tetrameric cytidine deaminase from Bacillus subtilis at 2.0 Å resolution. Biochemistry 41, 2563-2570 (2002).
    • (2002) Biochemistry , vol.41 , pp. 2563-2570
    • Johansson, E.1    Mejlhede, N.2    Neuhard, J.3    Larsen, S.4
  • 9
    • 2542542827 scopus 로고    scopus 로고
    • The structure of a yeast RNA-editing deaminase provides insight into the fold and function of activation-induced deaminase and APOBEC-1
    • Xie, K. et al. The structure of a yeast RNA-editing deaminase provides insight into the fold and function of activation-induced deaminase and APOBEC-1. Proc. Natl Acad. Sci. USA 101, 8114-8119 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 8114-8119
    • Xie, K.1
  • 10
    • 33746917191 scopus 로고    scopus 로고
    • The 1.48 Å resolution crystal structure of the homotetrameric cytidine deaminase from mouse
    • Teh, A. et al. The 1.48 Å resolution crystal structure of the homotetrameric cytidine deaminase from mouse. Biochemistry 45, 7825-7833 (2006).
    • (2006) Biochemistry , vol.45 , pp. 7825-7833
    • Teh, A.1
  • 11
    • 13444265938 scopus 로고    scopus 로고
    • Structure of human cytidine deaminase bound to a potent inhibitor
    • Chung, S. J., Fromme, J. C. & Verdine, G. L. Structure of human cytidine deaminase bound to a potent inhibitor. J. Med. Chem. 48, 658-660 (2005).
    • (2005) J. Med. Chem , vol.48 , pp. 658-660
    • Chung, S.J.1    Fromme, J.C.2    Verdine, G.L.3
  • 12
    • 0028057520 scopus 로고
    • Cytidine deaminase. The 2.3 Å crystal structure of an enzyme: Transition-state analog complex
    • Betts, L., Xiang, S., Short, S. A., Wolfenden, R. & Carter, C. W. Cytidine deaminase. The 2.3 Å crystal structure of an enzyme: transition-state analog complex. Curr. Biol. 235, 635-656 (1994).
    • (1994) Curr. Biol , vol.235 , pp. 635-656
    • Betts, L.1    Xiang, S.2    Short, S.A.3    Wolfenden, R.4    Carter, C.W.5
  • 13
    • 0028246560 scopus 로고
    • Mutations affecting transition-state stabilization by residues coordinating zinc at the active site of cytidine deaminase
    • Smith, A. A., Carlow, D. C., Wolfenden, R. & Short, S. A. Mutations affecting transition-state stabilization by residues coordinating zinc at the active site of cytidine deaminase. Biochemistry 33, 6468-6474 (1994).
    • (1994) Biochemistry , vol.33 , pp. 6468-6474
    • Smith, A.A.1    Carlow, D.C.2    Wolfenden, R.3    Short, S.A.4
  • 15
    • 0033669973 scopus 로고    scopus 로고
    • Mutations in activation-induced cytidine deaminase in patients with hyper IgM syndrome
    • Minegishi, Y. et al. Mutations in activation-induced cytidine deaminase in patients with hyper IgM syndrome. Clin. Immunol. 97, 203-210 (2000).
    • (2000) Clin. Immunol , vol.97 , pp. 203-210
    • Minegishi, Y.1
  • 16
    • 0035658430 scopus 로고    scopus 로고
    • ARCD-1, an apobec-1-related cytidine deaminase, exerts a dominant negative effect on C to U RNA editing
    • Anant, S. et al. ARCD-1, an apobec-1-related cytidine deaminase, exerts a dominant negative effect on C to U RNA editing. Am. J. Cell Physiol. 281, C1904-C1916 (2001).
    • (2001) Am. J. Cell Physiol , vol.281
    • Anant, S.1
  • 17
    • 0036200070 scopus 로고    scopus 로고
    • An anthropoid-specific locus of orphan C to U RNA-editing enzymes on chromosome 22
    • Jarmuz, A. et al. An anthropoid-specific locus of orphan C to U RNA-editing enzymes on chromosome 22. Genomics 79, 285-296 (2002).
    • (2002) Genomics , vol.79 , pp. 285-296
    • Jarmuz, A.1
  • 18
    • 0242497878 scopus 로고    scopus 로고
    • The enzymatic activity of CEM15/Apobec-3G is essential for the regulation of the infectivity of HIV-1 virion but not a sole determinant of its antiviral activity
    • Shindo, K. et al. The enzymatic activity of CEM15/Apobec-3G is essential for the regulation of the infectivity of HIV-1 virion but not a sole determinant of its antiviral activity. J. Biol. Chem. 278, 44412-44416 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 44412-44416
    • Shindo, K.1
  • 19
    • 3242712200 scopus 로고    scopus 로고
    • A second human antiretroviral factor, APOBEC3F, is suppressed by the HIV-1 and HIV-2 Vif proteins
    • Wiegand, H. L., Doehle, B. P., Bogerd, H. P. & Cullen, B. R. A second human antiretroviral factor, APOBEC3F, is suppressed by the HIV-1 and HIV-2 Vif proteins. EMBO J. 23, 2451-2458 (2004).
    • (2004) EMBO J , vol.23 , pp. 2451-2458
    • Wiegand, H.L.1    Doehle, B.P.2    Bogerd, H.P.3    Cullen, B.R.4
  • 20
    • 33646443637 scopus 로고    scopus 로고
    • Monomeric APOBEC3G is catalytically active and has antiviral activity
    • Opi, S. et al. Monomeric APOBEC3G is catalytically active and has antiviral activity. J. Virol. 80, 4673-4682 (2006).
    • (2006) J. Virol , vol.80 , pp. 4673-4682
    • Opi, S.1
  • 21
    • 13844270834 scopus 로고    scopus 로고
    • Complementary function of the two catalytic domains of APOBEC3G
    • Navarro, F. et al. Complementary function of the two catalytic domains of APOBEC3G. Virology 333, 374-386 (2005).
    • (2005) Virology , vol.333 , pp. 374-386
    • Navarro, F.1
  • 22
    • 84945509895 scopus 로고    scopus 로고
    • Identification of a specific domain required for dimerization of activation-induced cytidine deaminase
    • in the press
    • Wang, J. et al. Identification of a specific domain required for dimerization of activation-induced cytidine deaminase. J. Biol. Chem. (in the press).
    • J. Biol. Chem
    • Wang, J.1
  • 23
    • 0032958220 scopus 로고    scopus 로고
    • Mutational analysis of apolipoprotein B mRNA editing enzyme (APOBEC1): Structure-function relationships of RNA editing and dimerization
    • Teng, B. et al. Mutational analysis of apolipoprotein B mRNA editing enzyme (APOBEC1): structure-function relationships of RNA editing and dimerization. J. Lipid Res. 40, 623-635 (1999).
    • (1999) J. Lipid Res , vol.40 , pp. 623-635
    • Teng, B.1
  • 24
    • 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, 307-326 (1997).
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 25
    • 0033119895 scopus 로고    scopus 로고
    • Automated MAD and MIR structure solution
    • Terwilliger, T. C. & Berendzen, J. Automated MAD and MIR structure solution. Acta Crystallogr. 55, 849-861 (1999).
    • (1999) Acta Crystallogr , vol.55 , pp. 849-861
    • Terwilliger, T.C.1    Berendzen, J.2
  • 26
    • 0036793095 scopus 로고    scopus 로고
    • Substructure solution with SHELXD
    • Schneider, T. R. & Sheldrick, G. M. Substructure solution with SHELXD. Acta Crystallogr. 58, 1772-1779 (2002).
    • (2002) Acta Crystallogr , vol.58 , pp. 1772-1779
    • Schneider, T.R.1    Sheldrick, G.M.2
  • 27
    • 0033896691 scopus 로고    scopus 로고
    • Maximum-likelihood density modification
    • Terwilliger, T. C. Maximum-likelihood density modification. Acta Crystallogr. 56, 965-972 (2000).
    • (2000) Acta Crystallogr , vol.56 , pp. 965-972
    • Terwilliger, T.C.1
  • 28
    • 0037388165 scopus 로고    scopus 로고
    • Activation-induced cytidine deaminase deaminates deoxycytidine on single-stranded DNA but requires the action of RNase
    • Bransteitter, R., Pham, P., Scharff, M. D. & Goodman, M. F. Activation-induced cytidine deaminase deaminates deoxycytidine on single-stranded DNA but requires the action of RNase. Proc. Natl Acad. Sci. USA 100, 4102-4107 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 4102-4107
    • Bransteitter, R.1    Pham, P.2    Scharff, M.D.3    Goodman, M.F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.