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Volumn 18, Issue 2, 2011, Pages 222-227

Dynamic local unfolding in the serpin α-1 antitrypsin provides a mechanism for loop insertion and polymerization

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA 1 ANTITRYPSIN; CYSTEINE; SERINE PROTEINASE INHIBITOR;

EID: 79551646854     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.1976     Document Type: Article
Times cited : (47)

References (37)
  • 1
    • 0036882395 scopus 로고    scopus 로고
    • Serpin structure, mechanism, and function
    • Gettins, P.G. Serpin structure, mechanism, and function. Chem. Rev. 102, 4751-4804 (2002).
    • (2002) Chem. Rev. , vol.102 , pp. 4751-4804
    • Gettins, P.G.1
  • 2
    • 0034687422 scopus 로고    scopus 로고
    • Structure of a serpin-protease complex shows inhibition by deformation
    • Huntington, J.A., Read, R.J. & Carrell, R.W. Structure of a serpin-protease complex shows inhibition by deformation. Nature 407, 923-926 (2000).
    • (2000) Nature , vol.407 , pp. 923-926
    • Huntington, J.A.1    Read, R.J.2    Carrell, R.W.3
  • 3
    • 63849264516 scopus 로고    scopus 로고
    • Biochemical properties of plasminogen activator inhibitor-1
    • Dupont, D.M. et al. Biochemical properties of plasminogen activator inhibitor-1. Front. Biosci. 14, 1337-1361 (2009).
    • (2009) Front. Biosci. , vol.14 , pp. 1337-1361
    • Dupont, D.M.1
  • 4
    • 13244269951 scopus 로고    scopus 로고
    • Latent antithrombin and its detection, formation and turnover in the circulation
    • Mushunje, A., Evans, G., Brennan, S.O., Carrell, R.W. & Zhou, A. Latent antithrombin and its detection, formation and turnover in the circulation. J. Thromb. Haemost. 2, 2170-2177 (2004).
    • (2004) J. Thromb. Haemost. , vol.2 , pp. 2170-2177
    • Mushunje, A.1    Evans, G.2    Brennan, S.O.3    Carrell, R.W.4    Zhou, A.5
  • 5
    • 0030982322 scopus 로고    scopus 로고
    • Effects of serpin binding on the target proteinase: Global stabilization, localized increased structural fexibility, and conserved hydrogen bonding at the active site
    • Kaslik, G. et al. Effects of serpin binding on the target proteinase: global stabilization, localized increased structural fexibility, and conserved hydrogen bonding at the active site. Biochemistry 36, 5455-5464 (1997).
    • (1997) Biochemistry , vol.36 , pp. 5455-5464
    • Kaslik, G.1
  • 6
    • 0030475698 scopus 로고    scopus 로고
    • Kinetically controlled folding of the serpin plasminogen activator inhibitor 1
    • Wang, Z., Mottonen, J. & Goldsmith, E.J. Kinetically controlled folding of the serpin plasminogen activator inhibitor 1. Biochemistry 35, 16443-16448 (1996).
    • (1996) Biochemistry , vol.35 , pp. 16443-16448
    • Wang, Z.1    Mottonen, J.2    Goldsmith, E.J.3
  • 7
    • 67650713938 scopus 로고    scopus 로고
    • Conformational pathology of the serpins: Themes, variations, and therapeutic strategies
    • Gooptu, B. & Lomas, D.A. Conformational pathology of the serpins: themes, variations, and therapeutic strategies. Annu. Rev. Biochem. 78, 147-176 (2009).
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 147-176
    • Gooptu, B.1    Lomas, D.A.2
  • 8
    • 0035862204 scopus 로고    scopus 로고
    • The folding of α-1-proteinase inhibitor: Kinetic vs equilibrium control
    • Tran, S.T. & Shrake, A. The folding of α-1-proteinase inhibitor: kinetic vs equilibrium control. Arch. Biochem. Biophys. 385, 322-331 (2001).
    • (2001) Arch. Biochem. Biophys. , vol.385 , pp. 322-331
    • Tran, S.T.1    Shrake, A.2
  • 9
    • 55249111481 scopus 로고    scopus 로고
    • Crystal structure of a stable dimer reveals the molecular basis of serpin polymerization
    • Yamasaki, M., Li, W., Johnson, D.J. & Huntington, J.A. Crystal structure of a stable dimer reveals the molecular basis of serpin polymerization. Nature 455, 1255-1258 (2008).
    • (2008) Nature , vol.455 , pp. 1255-1258
    • Yamasaki, M.1    Li, W.2    Johnson, D.J.3    Huntington, J.A.4
  • 10
    • 77957251912 scopus 로고    scopus 로고
    • The loop-sheet mechanism of serpin polymerization tested by reactive center loop mutations
    • Yamasaki, M., Sendall, T.J., Harris, L.E., Lewis, G.M. & Huntington, J.A. The loop-sheet mechanism of serpin polymerization tested by reactive center loop mutations. J. Biol. Chem. 285, 30752-30758 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 30752-30758
    • Yamasaki, M.1    Sendall, T.J.2    Harris, L.E.3    Lewis, G.M.4    Huntington, J.A.5
  • 11
    • 78049239444 scopus 로고    scopus 로고
    • Defning the mechanism of polymerization in the serpinopathies
    • Ekeowa, U.I. et al. Defning the mechanism of polymerization in the serpinopathies. Proc. Natl. Acad. Sci. USA 107, 17146-17151 (2010).
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 17146-17151
    • Ekeowa, U.I.1
  • 13
    • 0037046167 scopus 로고    scopus 로고
    • Probing the role of the F-helix in serpin stability through a single tryptophan substitution
    • Cabrita, L.D., Whisstock, J.C. & Bottomley, S.P. Probing the role of the F-helix in serpin stability through a single tryptophan substitution. Biochemistry 41, 4575-4581 (2002).
    • (2002) Biochemistry , vol.41 , pp. 4575-4581
    • Cabrita, L.D.1    Whisstock, J.C.2    Bottomley, S.P.3
  • 14
    • 55249112306 scopus 로고    scopus 로고
    • Serpins' mystery solved
    • Whisstock, J.C. & Bottomley, S.P. Serpins' mystery solved. Nature 455, 1189-1190 (2008).
    • (2008) Nature , vol.455 , pp. 1189-1190
    • Whisstock, J.C.1    Bottomley, S.P.2
  • 15
    • 34447104835 scopus 로고    scopus 로고
    • Cooperative unfolding of a metastable serpin to a molten globule suggests a link between functional and folding energy landscapes
    • Tsutsui, Y. & Wintrode, P.L. Cooperative unfolding of a metastable serpin to a molten globule suggests a link between functional and folding energy landscapes. J. Mol. Biol. 371, 245-255 (2007).
    • (2007) J. Mol. Biol. , vol.371 , pp. 245-255
    • Tsutsui, Y.1    Wintrode, P.L.2
  • 16
    • 0001268827 scopus 로고    scopus 로고
    • Distribution of the native strain in human α 1-antitrypsin and its association with protease inhibitor function
    • Seo, E.J., Im, H., Maeng, J.S., Kim, K.E. & Yu, M.H. Distribution of the native strain in human α 1-antitrypsin and its association with protease inhibitor function. J. Biol. Chem. 275, 16904-16909 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 16904-16909
    • Seo, E.J.1    Im, H.2    Maeng, J.S.3    Kim, K.E.4    Yu, M.H.5
  • 17
    • 0035818431 scopus 로고    scopus 로고
    • PEGylation: A method for assessing topological accessibilities in Kv1.3
    • Lu, J. & Deutsch, C. PEGylation: a method for assessing topological accessibilities in Kv1.3. Biochemistry 40, 13288-13301 (2001).
    • (2001) Biochemistry , vol.40 , pp. 13288-13301
    • Lu, J.1    Deutsch, C.2
  • 18
    • 0032500811 scopus 로고    scopus 로고
    • Alpha 1-antitrypsin polymerisation can occur by both loop A and C sheet mechanisms
    • Bottomley, S.P., Hopkins, P.C. & Whisstock, J.C. Alpha 1-antitrypsin polymerisation can occur by both loop A and C sheet mechanisms. Biochem. Biophys. Res. Commun. 251, 1-5 (1998).
    • (1998) Biochem. Biophys. Res. Commun. , vol.251 , pp. 1-5
    • Bottomley, S.P.1    Hopkins, P.C.2    Whisstock, J.C.3
  • 19
    • 0035834481 scopus 로고    scopus 로고
    • Probing the equilibrium denaturation of the serpin α (1)-antitrypsin with single tryptophan mutants; Evidence for structure in the urea unfolded state
    • Tew, D.J. & Bottomley, S.P. Probing the equilibrium denaturation of the serpin α (1)-antitrypsin with single tryptophan mutants; evidence for structure in the urea unfolded state. J. Mol. Biol. 313, 1161-1169 (2001).
    • (2001) J. Mol. Biol. , vol.313 , pp. 1161-1169
    • Tew, D.J.1    Bottomley, S.P.2
  • 20
    • 0026504260 scopus 로고
    • Effects of glycosylation on the folding and stability of human, recombinant and cleaved α 1-antitrypsin
    • Powell, L.M. & Pain, R.H. Effects of glycosylation on the folding and stability of human, recombinant and cleaved α 1-antitrypsin. J. Mol. Biol. 224, 241-252 (1992).
    • (1992) J. Mol. Biol. , vol.224 , pp. 241-252
    • Powell, L.M.1    Pain, R.H.2
  • 22
    • 0024217519 scopus 로고
    • Repair of the secretion defect in the Z form of α 1-antitrypsin by addition of a second mutation
    • Brantly, M., Courtney, M. & Crystal, R.G. Repair of the secretion defect in the Z form of α 1-antitrypsin by addition of a second mutation. Science 242, 1700-1702 (1988).
    • (1988) Science , vol.242 , pp. 1700-1702
    • Brantly, M.1    Courtney, M.2    Crystal, R.G.3
  • 23
    • 0038053035 scopus 로고    scopus 로고
    • Serpin polymerization is prevented by a hydrogen bond network that is centered on His-334 and stabilized by glycerol
    • Zhou, A., Stein, P.E., Huntington, J.A. & Carrell, R.W. Serpin polymerization is prevented by a hydrogen bond network that is centered on His-334 and stabilized by glycerol. J. Biol. Chem. 278, 15116-15122 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 15116-15122
    • Zhou, A.1    Stein, P.E.2    Huntington, J.A.3    Carrell, R.W.4
  • 24
    • 0028908402 scopus 로고
    • A thermostable mutation located at the hydrophobic core of α 1-antitrypsin suppresses the folding defect of the Z-type variant
    • Kim, J., Lee, K.N., Yi, G.S. & Yu, M.H. A thermostable mutation located at the hydrophobic core of α 1-antitrypsin suppresses the folding defect of the Z-type variant. J. Biol. Chem. 270, 8597-8601 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 8597-8601
    • Kim, J.1    Lee, K.N.2    Yi, G.S.3    Yu, M.H.4
  • 25
    • 61649086681 scopus 로고    scopus 로고
    • A1ATVar: A relational database of human SERPINA1 gene variants leading to α1-antitrypsin defciency and application of the VariVis software
    • Zaimidou, S. et al. A1ATVar: a relational database of human SERPINA1 gene variants leading to α1-antitrypsin defciency and application of the VariVis software. Hum. Mutat. 30, 308-313 (2009).
    • (2009) Hum. Mutat. , vol.30 , pp. 308-313
    • Zaimidou, S.1
  • 26
    • 70349446583 scopus 로고    scopus 로고
    • Expression, purifcation and characterization of recombinant Z α (1)-antitrypsin - The most common cause of α (1)-antitrypsin defciency
    • Levina, V. et al. Expression, purifcation and characterization of recombinant Z α (1)-antitrypsin-the most common cause of α (1)-antitrypsin defciency. Protein Expr. Purif. 68, 226-232 (2009).
    • (2009) Protein Expr. Purif. , vol.68 , pp. 226-232
    • Levina, V.1
  • 27
    • 0027534475 scopus 로고
    • Rare α 1 antitrypsin allele PI W and a history of infant liver disease
    • Clark, P. & Chong, A.Y. Rare α 1 antitrypsin allele PI W and a history of infant liver disease. Am. J. Med. Genet. 45, 674-676 (1993).
    • (1993) Am. J. Med. Genet. , vol.45 , pp. 674-676
    • Clark, P.1    Chong, A.Y.2
  • 28
    • 0029048542 scopus 로고
    • The Z type variation of human α 1-antitrypsin causes a protein folding defect
    • Yu, M.H., Lee, K.N. & Kim, J. The Z type variation of human α 1-antitrypsin causes a protein folding defect. Nat. Struct. Biol. 2, 363-367 (1995).
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 363-367
    • Yu, M.H.1    Lee, K.N.2    Kim, J.3
  • 29
    • 0029842156 scopus 로고    scopus 로고
    • New insights into the structural basis of α 1-antitrypsin defciency
    • Lomas, D.A. New insights into the structural basis of α 1-antitrypsin defciency. Q. J. Med. 89, 807-812 (1996).
    • (1996) Q. J. Med. , vol.89 , pp. 807-812
    • Lomas, D.A.1
  • 30
    • 19944430698 scopus 로고    scopus 로고
    • Polymers of Z α1-antitrypsin co-localize with neutrophils in emphysematous alveoli and are chemotactic in vivo
    • Mahadeva, R. et al. Polymers of Z α1-antitrypsin co-localize with neutrophils in emphysematous alveoli and are chemotactic in vivo. Am. J. Pathol. 166, 377-386 (2005).
    • (2005) Am. J. Pathol. , vol.166 , pp. 377-386
    • Mahadeva, R.1
  • 31
    • 0343193210 scopus 로고    scopus 로고
    • Topography of a 2.0 Å structure of α1-antitrypsin reveals targets for rational drug design to prevent conformational disease
    • Elliott, P.R., Pei, X.Y., Dafforn, T.R. & Lomas, D.A. Topography of a 2.0 Å structure of α1-antitrypsin reveals targets for rational drug design to prevent conformational disease. Protein Sci. 9, 1274-1281 (2000).
    • (2000) Protein Sci. , vol.9 , pp. 1274-1281
    • Elliott, P.R.1    Pei, X.Y.2    Dafforn, T.R.3    Lomas, D.A.4
  • 33
    • 33748588165 scopus 로고    scopus 로고
    • Inhibition of protein aggregation in vitro and in vivo by a natural osmoprotectant
    • Ignatova, Z. & Gierasch, L.M. Inhibition of protein aggregation in vitro and in vivo by a natural osmoprotectant. Proc. Natl. Acad. Sci. USA 103, 13357-13361 (2006).
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 13357-13361
    • Ignatova, Z.1    Gierasch, L.M.2
  • 34
    • 0028915773 scopus 로고
    • Perturbation of a tertiary hydrogen bond in barstar by mutagenesis of the sole His residue to Gln leads to accumulation of at least one equilibrium folding intermediate
    • Nath, U. & Udgaonkar, J.B. Perturbation of a tertiary hydrogen bond in barstar by mutagenesis of the sole His residue to Gln leads to accumulation of at least one equilibrium folding intermediate. Biochemistry 34, 1702-1713 (1995).
    • (1995) Biochemistry , vol.34 , pp. 1702-1713
    • Nath, U.1    Udgaonkar, J.B.2
  • 35
    • 0025949415 scopus 로고
    • Reexamination of the folding of BPTI: Predominance of native intermediates
    • Weissman, J.S. & Kim, P.S. Reexamination of the folding of BPTI: predominance of native intermediates. Science 253, 1386-1393 (1991).
    • (1991) Science , vol.253 , pp. 1386-1393
    • Weissman, J.S.1    Kim, P.S.2
  • 36
    • 69949093360 scopus 로고    scopus 로고
    • An introduction to methods for analyzing thiols and disulfdes: Reactions, reagents, and practical considerations
    • Hansen, R.E. & Winther, J.R. An introduction to methods for analyzing thiols and disulfdes: Reactions, reagents, and practical considerations. Anal. Biochem. 394, 147-158 (2009).
    • (2009) Anal. Biochem. , vol.394 , pp. 147-158
    • Hansen, R.E.1    Winther, J.R.2
  • 37
    • 38649084667 scopus 로고    scopus 로고
    • Functional site profling and electrostatic analysis of cysteines modifable to cysteine sulfenic acid
    • Salsbury, F.R. Jr, Knutson, S.T., Poole, L.B. & Fetrow, J.S. Functional site profling and electrostatic analysis of cysteines modifable to cysteine sulfenic acid. Protein Sci. 17, 299-312 (2008).
    • (2008) Protein Sci. , vol.17 , pp. 299-312
    • Salsbury Jr., F.R.1    Knutson, S.T.2    Poole, L.B.3    Fetrow, J.S.4


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