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Volumn 7, Issue 6, 2010, Pages 404-407

The folding pathway of a1-antitrypsin: Avoiding the unavoidable

Author keywords

Protein aggregation; Protein folding; Serpin; 1 antitrypsin

Indexed keywords

ALPHA 1 ANTITRYPSIN;

EID: 79952680796     PISSN: 15463222     EISSN: 19435665     Source Type: Journal    
DOI: 10.1513/pats.201004-031AW     Document Type: Conference Paper
Times cited : (6)

References (40)
  • 1
    • 34447095724 scopus 로고    scopus 로고
    • Molecular gymnastics: Serpin structure, folding and misfolding
    • Whisstock JC, Bottomley SP. Molecular gymnastics: serpin structure, folding and misfolding. Curr Opin Struct Biol 2006;16:761-768.
    • (2006) Curr Opin Struct Biol , vol.16 , pp. 761-768
    • Whisstock, J.C.1    Bottomley, S.P.2
  • 2
    • 67650713938 scopus 로고    scopus 로고
    • Conformational pathology of the serpins: Themes, variations, and therapeutic strategies
    • Gooptu B, Lomas DA. Conformational pathology of the serpins: themes, variations, and therapeutic strategies. Annu Rev Biochem 2009;78:147-176.
    • (2009) Annu Rev Biochem , vol.78 , pp. 147-176
    • Gooptu, B.1    Lomas, D.A.2
  • 3
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen CB. Principles that govern the folding of protein chains. Science 1973;181:223-230.
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 4
    • 3042617720 scopus 로고    scopus 로고
    • How do proteins avoid becoming too stable? Biophysical studies into metastable proteins
    • Cabrita LD, Bottomley SP. How do proteins avoid becoming too stable? Biophysical studies into metastable proteins. Eur Biophys J 2004;33: 83-88.
    • (2004) Eur Biophys J , vol.33 , pp. 83-88
    • Cabrita, L.D.1    Bottomley, S.P.2
  • 5
    • 0034523345 scopus 로고    scopus 로고
    • Phylogeny of the serpin superfamily: Implications of patterns of amino acid conservation for structure and function
    • Irving JA, Pike RN, Lesk AM, Whisstock JC. Phylogeny of the serpin superfamily: implications of patterns of amino acid conservation for structure and function. Genome Res 2000;10:1841-1860.
    • (2000) Genome Res , vol.10 , pp. 1841-1860
    • Irving, J.A.1    Pike, R.N.2    Lesk, A.M.3    Whisstock, J.C.4
  • 6
    • 17744409446 scopus 로고    scopus 로고
    • Wild-type alpha 1-antitrypsin is in the canonical inhibitory conformation
    • Elliott PR, Abrahams JP, Lomas DA. Wild-type alpha 1-antitrypsin is in the canonical inhibitory conformation. J Mol Biol 1998;275:419-425.
    • (1998) J Mol Biol , vol.275 , pp. 419-425
    • Elliott, P.R.1    Abrahams, J.P.2    Lomas, D.A.3
  • 7
    • 0034687422 scopus 로고    scopus 로고
    • Structure of a serpin-protease complex shows inhibition by deformation
    • Huntington JA, Read RJ, Carrell RW. Structure of a serpin-protease complex shows inhibition by deformation. Nature 2000;407:923-926.
    • (2000) Nature , vol.407 , pp. 923-926
    • Huntington, J.A.1    Read, R.J.2    Carrell, R.W.3
  • 8
    • 0033608984 scopus 로고    scopus 로고
    • Formation of the covalent serpin-proteinase complex involves translocation of the proteinase by more than 70 A and full insertion of the reactive center loop into beta-sheet A
    • Stratikos E, Gettins PG. Formation of the covalent serpin-proteinase complex involves translocation of the proteinase by more than 70 A and full insertion of the reactive center loop into beta-sheet A. Proc Natl Acad Sci USA 1999;96:4808-4813.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 4808-4813
    • Stratikos, E.1    Gettins, P.G.2
  • 9
    • 0035815470 scopus 로고    scopus 로고
    • Intrinsic fluorescence changes and rapid kinetics of proteinase deformation during serpin inhibition
    • Tew DJ, Bottomley SP. Intrinsic fluorescence changes and rapid kinetics of proteinase deformation during serpin inhibition. FEBS Lett 2001; 494:30-33.
    • (2001) FEBS Lett , vol.494 , pp. 30-33
    • Tew, D.J.1    Bottomley, S.P.2
  • 10
    • 0023700976 scopus 로고
    • Plasma serine proteinase inhibitors (serpins) exhibit major conformational changes and a large increase in conformational stability upon cleavage at their reactive sites
    • Bruch M, Weiss V, Engel J. Plasma serine proteinase inhibitors (serpins) exhibit major conformational changes and a large increase in conformational stability upon cleavage at their reactive sites. J Biol Chem 1988;263:16626-16630.
    • (1988) J Biol Chem , vol.263 , pp. 16626-16630
    • Bruch, M.1    Weiss, V.2    Engel, J.3
  • 11
    • 0026504260 scopus 로고
    • Effects of glycosylation on the folding and stability of human, recombinant and cleaved alpha 1-antitrypsin
    • Powell LM, Pain RH. Effects of glycosylation on the folding and stability of human, recombinant and cleaved alpha 1-antitrypsin. J Mol Biol 1992;224:241-252.
    • (1992) J Mol Biol , vol.224 , pp. 241-252
    • Powell, L.M.1    Pain, R.H.2
  • 12
    • 0025087931 scopus 로고
    • Conformational changes in intact and papainmodified alpha 1-proteinase inhibitor induced by guanidinium chloride
    • Herve M, Ghelis C. Conformational changes in intact and papainmodified alpha 1-proteinase inhibitor induced by guanidinium chloride. Eur J Biochem 1990;191:653-658.
    • (1990) Eur J Biochem , vol.191 , pp. 653-658
    • Herve, M.1    Ghelis, C.2
  • 13
    • 0021747157 scopus 로고
    • Human alpha 1-proteinase inhibitor: Crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function
    • Loebermann H, Tokuoka R, Deisenhofer J, Huber R. Human alpha 1-proteinase inhibitor: crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function. J Mol Biol 1984;177:531-557.
    • (1984) J Mol Biol , vol.177 , pp. 531-557
    • Loebermann, H.1    Tokuoka, R.2    Deisenhofer, J.3    Huber, R.4
  • 14
    • 0034602778 scopus 로고    scopus 로고
    • Inactive conformation of the serpin alpha(1)-antichymotrypsin indicates two-stage insertion of the reactive loop: Implications for inhibitory function and conformational disease
    • Gooptu B, Hazes B, Chang WS, Dafforn TR, Carrell RW, Read RJ, Lomas DA. Inactive conformation of the serpin alpha(1)-antichymotrypsin indicates two-stage insertion of the reactive loop: implications for inhibitory function and conformational disease. Proc Natl Acad Sci USA 2000;97:67-72.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 67-72
    • Gooptu, B.1    Hazes, B.2    Chang, W.S.3    Dafforn, T.R.4    Carrell, R.W.5    Read, R.J.6    Lomas, D.A.7
  • 16
    • 0029589824 scopus 로고
    • What do dysfunctional serpins tell us about molecular mobility and disease?
    • Stein PE, Carrell RW. What do dysfunctional serpins tell us about molecular mobility and disease? Nat Struct Biol 1995;2:96-113.
    • (1995) Nat Struct Biol , vol.2 , pp. 96-113
    • Stein, P.E.1    Carrell, R.W.2
  • 17
    • 34848911346 scopus 로고    scopus 로고
    • Aeropin from the extremophile Pyrobaculum aerophilum bypasses the serpin misfolding trap
    • Cabrita LD, Irving JA, Pearce MC, Whisstock JC, Bottomley SP. Aeropin from the extremophile Pyrobaculum aerophilum bypasses the serpin misfolding trap. J Biol Chem 2007;282:26802-26809.
    • (2007) J Biol Chem , vol.282 , pp. 26802-26809
    • Cabrita, L.D.1    Irving, J.A.2    Pearce, M.C.3    Whisstock, J.C.4    Bottomley, S.P.5
  • 18
    • 1542496192 scopus 로고    scopus 로고
    • The 1.5 a crystal structure of a prokaryote serpin: Controlling conformational change in a heated environment
    • Irving JA, Cabrita LD, Rossjohn J, Pike RN, Bottomley SP, Whisstock JC. The 1.5 a crystal structure of a prokaryote serpin: controlling conformational change in a heated environment. Structure 2003;11:387-397.
    • (2003) Structure , vol.11 , pp. 387-397
    • Irving, J.A.1    Cabrita, L.D.2    Rossjohn, J.3    Pike, R.N.4    Bottomley, S.P.5    Whisstock, J.C.6
  • 19
    • 0034665989 scopus 로고    scopus 로고
    • Conformational change and intermediates in the unfolding of falphag1-antichymotrypsin
    • Pearce MC, Rubin H, Bottomley SP. Conformational change and intermediates in the unfolding of falphag1-antichymotrypsin. J Biol Chem 2000;275:28513-28518.
    • (2000) J Biol Chem , vol.275 , pp. 28513-28518
    • Pearce, M.C.1    Rubin, H.2    Bottomley, S.P.3
  • 21
    • 0027958069 scopus 로고
    • The use of fluorescence methods to monitor unfolding transitions in proteins
    • Eftink MR. The use of fluorescence methods to monitor unfolding transitions in proteins. Biophys J 1994;66:482-501.
    • (1994) Biophys J , vol.66 , pp. 482-501
    • Eftink, M.R.1
  • 23
    • 0035834481 scopus 로고    scopus 로고
    • Probing the equilibrium denaturation of the serpin alpha(1)-antitrypsin with single tryptophan mutants; Evidence for structure in the urea unfolded state
    • Tew DJ, Bottomley SP. Probing the equilibrium denaturation of the serpin alpha(1)-antitrypsin with single tryptophan mutants; evidence for structure in the urea unfolded state. J Mol Biol 2001;313:1161-1169.
    • (2001) J Mol Biol , vol.313 , pp. 1161-1169
    • Tew, D.J.1    Bottomley, S.P.2
  • 24
    • 3342889562 scopus 로고    scopus 로고
    • Different conformational changes within the F-helix occur during serpin folding, polymerization, and proteinase inhibition
    • Cabrita LD, Dai W, Bottomley SP. Different conformational changes within the F-helix occur during serpin folding, polymerization, and proteinase inhibition. Biochemistry 2004;43:9834-9839.
    • (2004) Biochemistry , vol.43 , pp. 9834-9839
    • Cabrita, L.D.1    Dai, W.2    Bottomley, S.P.3
  • 25
    • 0037046167 scopus 로고    scopus 로고
    • Probing the role of the F-helix in serpin stability through a single tryptophan substitution
    • Cabrita LD, Whisstock JC, Bottomley SP. Probing the role of the F-helix in serpin stability through a single tryptophan substitution. Biochemistry 2002;41:4575-4581.
    • (2002) Biochemistry , vol.41 , pp. 4575-4581
    • Cabrita, L.D.1    Whisstock, J.C.2    Bottomley, S.P.3
  • 26
    • 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 PL. Cooperative unfolding of a metastable serpin to a molten globule suggests a link between functional and folding energy landscapes. J Mol Biol 2007;371:245-255.
    • (2007) J Mol Biol , vol.371 , pp. 245-255
    • Tsutsui, Y.1    Wintrode, P.L.2
  • 27
    • 0001268827 scopus 로고    scopus 로고
    • Distribution of the native strain in human alpha 1-antitrypsin and its association with protease inhibitor function
    • Seo EJ, Im H, Maeng JS, Kim KE, Yu MH. Distribution of the native strain in human alpha 1-antitrypsin and its association with protease inhibitor function. J Biol Chem 2000;275:16904-16909.
    • (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
  • 28
    • 0029994816 scopus 로고    scopus 로고
    • Probing the native strain iin alpha1-antitrypsin
    • Lee KN, Park SD, Yu MH. Probing the native strain iin alpha1-antitrypsin. Nat Struct Biol 1996;3:497-500.
    • (1996) Nat Struct Biol , vol.3 , pp. 497-500
    • Lee, K.N.1    Park, S.D.2    Yu, M.H.3
  • 29
    • 0030587834 scopus 로고    scopus 로고
    • The native strains in the hydrophobic core and flexible reactive loop of a serine protease inhibitor: Crystal structure of an uncleaved alpha1-antitrypsin at 2.7A
    • Ryu SE, Choi HJ, Kwon KS, Lee KN, Yu MH. The native strains in the hydrophobic core and flexible reactive loop of a serine protease inhibitor: crystal structure of an uncleaved alpha1-antitrypsin at 2.7A . Structure 1996;4:1181-1192.
    • (1996) Structure , vol.4 , pp. 1181-1192
    • Ryu, S.E.1    Choi, H.J.2    Kwon, K.S.3    Lee, K.N.4    Yu, M.H.5
  • 30
    • 0344076056 scopus 로고    scopus 로고
    • Metastability in the inhibitory mechanism of human alpha1-antitrypsin
    • Im H, Seo EJ, Yu MH. Metastability in the inhibitory mechanism of human alpha1-antitrypsin. J Biol Chem 1999;274:11072-11077.
    • (1999) J Biol Chem , vol.274 , pp. 11072-11077
    • Im, H.1    Seo, E.J.2    Yu, M.H.3
  • 31
    • 0034608856 scopus 로고    scopus 로고
    • Regulation of protein function by native metastability
    • Lee C, Park SH, Lee MY, Yu MH. Regulation of protein function by native metastability. Proc Natl Acad Sci USA 2000;97: 7727-7731.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 7727-7731
    • Lee, C.1    Park, S.H.2    Lee, M.Y.3    Yu, M.H.4
  • 32
    • 0037195790 scopus 로고    scopus 로고
    • Interactions causing the kinetic trap in serpin protein folding
    • Im H, Woo MS, Hwang KY, Yu MH. Interactions causing the kinetic trap in serpin protein folding. J Biol Chem 2002;277:46347-46354.
    • (2002) J Biol Chem , vol.277 , pp. 46347-46354
    • Im, H.1    Woo, M.S.2    Hwang, K.Y.3    Yu, M.H.4
  • 33
    • 17544381846 scopus 로고    scopus 로고
    • A protein family under 'stress'-serpin stability, folding and misfolding
    • Devlin GL, Bottomley SP. A protein family under 'stress'-serpin stability, folding and misfolding. Front Biosci 2005;10:288-299.
    • (2005) Front Biosci , vol.10 , pp. 288-299
    • Devlin, G.L.1    Bottomley, S.P.2
  • 34
    • 0032085755 scopus 로고    scopus 로고
    • Genetics and respiratory disease 2 Alpha 1-antitrypsin deficiency, cirrhosis and emphysema
    • Mahadeva R, Lomas DA. Genetics and respiratory disease 2 Alpha 1-antitrypsin deficiency, cirrhosis and emphysema. Thorax 1998;53: 501-505.
    • (1998) Thorax , vol.53 , pp. 501-505
    • Mahadeva, R.1    Lomas, D.A.2
  • 35
    • 0026755363 scopus 로고
    • The mechanism of Z alpha 1-antitrypsin accumulation in the liver
    • Lomas DA, Evans DL, Finch JT, Carrell RW. The mechanism of Z alpha 1-antitrypsin accumulation in the liver. Nature 1992;357:605-607.
    • (1992) Nature , vol.357 , pp. 605-607
    • Lomas, D.A.1    Evans, D.L.2    Finch, J.T.3    Carrell, R.W.4
  • 36
    • 0027473016 scopus 로고
    • Effect of the Z mutation on the physical and inhibitory properties of alpha 1-antitrypsin
    • Lomas DA, Evans DL, Stone SR, Chang WS, Carrell RW. Effect of the Z mutation on the physical and inhibitory properties of alpha 1-antitrypsin. Biochemistry 1993;32:500-508.
    • (1993) Biochemistry , vol.32 , pp. 500-508
    • Lomas, D.A.1    Evans, D.L.2    Stone, S.R.3    Chang, W.S.4    Carrell, R.W.5
  • 37
    • 0036510604 scopus 로고    scopus 로고
    • 6-mer peptide selectively anneals to a pathogenic serpin conformation and blocks polymerization: Implications for the prevention of z alpha(1)-antitrypsin-related cirrhosis
    • Mahadeva R, Dafforn TR, Carrell RW, Lomas DA. 6-mer peptide selectively anneals to a pathogenic serpin conformation and blocks polymerization: implications for the prevention of z alpha(1)-antitrypsin-related cirrhosis. J Biol Chem 2002;277:6771-6774.
    • (2002) J Biol Chem , vol.277 , pp. 6771-6774
    • Mahadeva, R.1    Dafforn, T.R.2    Carrell, R.W.3    Lomas, D.A.4
  • 39
    • 0029048542 scopus 로고
    • The Z type variation of human alpha 1-antitrypsin causes a protein folding defect
    • Yu MH, Lee KN, Kim J. The Z type variation of human alpha 1-antitrypsin causes a protein folding defect. Nat Struct Biol 1995;2: 363-367.
    • (1995) Nat Struct Biol , vol.2 , pp. 363-367
    • Yu, M.H.1    Lee, K.N.2    Kim, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.