메뉴 건너뛰기




Volumn 348, Issue 2, 2005, Pages 409-418

Dynamic mechanism for the serpin loop insertion as revealed by quantitative kinetics

Author keywords

Loop insertion; Ovalbumin; Quantitative kinetics for serpin loop insertion; Serpins; Transition intermediate

Indexed keywords

OVALBUMIN; SERINE PROTEINASE INHIBITOR;

EID: 16244370412     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.02.054     Document Type: Article
Times cited : (3)

References (35)
  • 1
    • 0035823595 scopus 로고    scopus 로고
    • The serpins are an expanding superfamily of structurally similar but functionally diverse proteins. Evolution, mechanism of inhibition, novel functions, and a revised nomenclature
    • G.A. Silverman, P.I. Bird, R.W. Carrell, F.C. Church, P.B. Coughlin, and P.G. Gettins The serpins are an expanding superfamily of structurally similar but functionally diverse proteins. Evolution, mechanism of inhibition, novel functions, and a revised nomenclature J. Biol. Chem. 276 2001 33293 33296
    • (2001) J. Biol. Chem. , vol.276 , pp. 33293-33296
    • Silverman, G.A.1    Bird, P.I.2    Carrell, R.W.3    Church, F.C.4    Coughlin, P.B.5    Gettins, P.G.6
  • 2
    • 0036882395 scopus 로고    scopus 로고
    • Serpin structure, mechanism, and function
    • P.G. Gettins Serpin structure, mechanism, and function Chem. Rev. 102 2002 4751 4804
    • (2002) Chem. Rev. , vol.102 , pp. 4751-4804
    • Gettins, P.G.1
  • 3
    • 0036789017 scopus 로고    scopus 로고
    • Serpinopathies and the conformational dementias
    • D.A. Lomas, and R.W. Carrell Serpinopathies and the conformational dementias Nature Rev. Genet. 3 2002 759 768
    • (2002) Nature Rev. Genet. , vol.3 , pp. 759-768
    • Lomas, D.A.1    Carrell, R.W.2
  • 4
    • 0034687422 scopus 로고    scopus 로고
    • Structure of a serpin-protease complex shows inhibition by deformation
    • J.A. Huntington, R.J. Read, and R.W. Carrell Structure of a serpin-protease complex shows inhibition by deformation Nature 407 2000 923 926
    • (2000) Nature , vol.407 , pp. 923-926
    • Huntington, J.A.1    Read, R.J.2    Carrell, R.W.3
  • 5
    • 0022243864 scopus 로고
    • Endothelial cells produce a latent inhibitor of plasminogen activators that can be activated by denaturants
    • C.M. Hekman, and D.J. Loskutoff Endothelial cells produce a latent inhibitor of plasminogen activators that can be activated by denaturants J. Biol. Chem. 260 1985 11581 11587
    • (1985) J. Biol. Chem. , vol.260 , pp. 11581-11587
    • Hekman, C.M.1    Loskutoff, D.J.2
  • 7
    • 0028773279 scopus 로고
    • Biological implications of a 3 Å structure of dimeric antithrombin
    • R.W. Carrell, P.E. Stein, G. Fermi, and M.R. Wardell Biological implications of a 3 Å structure of dimeric antithrombin Structure 2 1994 257 270
    • (1994) Structure , vol.2 , pp. 257-270
    • Carrell, R.W.1    Stein, P.E.2    Fermi, G.3    Wardell, M.R.4
  • 11
    • 0024423930 scopus 로고
    • 1- antitrypsin for structure and function of serpins
    • 1-antitrypsin for structure and function of serpins Biochemistry 28 1989 8951 8966
    • (1989) Biochemistry , vol.28 , pp. 8951-8966
    • Huber, R.1    Carrell, R.W.2
  • 14
    • 0024557050 scopus 로고
    • Absence of large-scale conformational change upon limited proteolysis of ovalbumin, the prototypic serpin
    • P. Gettins Absence of large-scale conformational change upon limited proteolysis of ovalbumin, the prototypic serpin J. Biol. Chem. 264 1989 3781 3785
    • (1989) J. Biol. Chem. , vol.264 , pp. 3781-3785
    • Gettins, P.1
  • 15
    • 0024430428 scopus 로고
    • Ovalbumin and angiotensinogen lack serpin S-R conformational change
    • P.E. Stein, D.A. Tewkesbury, and R.W. Carrell Ovalbumin and angiotensinogen lack serpin S-R conformational change Biochem. J. 262 1989 103 107
    • (1989) Biochem. J. , vol.262 , pp. 103-107
    • Stein, P.E.1    Tewkesbury, D.A.2    Carrell, R.W.3
  • 16
    • 0030916868 scopus 로고    scopus 로고
    • Serpin conformational change in ovalbumin. Enhanced reactive center loop insertion through hinge region mutations
    • J.A. Huntington, B. Fan, K.E. Karlsson, J. Deinum, D.A. Lawrence, and P.G. Gettins Serpin conformational change in ovalbumin. Enhanced reactive center loop insertion through hinge region mutations Biochemistry 36 1997 5432 5440
    • (1997) Biochemistry , vol.36 , pp. 5432-5440
    • Huntington, J.A.1    Fan, B.2    Karlsson, K.E.3    Deinum, J.4    Lawrence, D.A.5    Gettins, P.G.6
  • 17
    • 0036298517 scopus 로고    scopus 로고
    • Loop-inserted and thermostabilized structure of P1-P1′ cleaved ovalbumin mutant R339T
    • M. Yamasaki, Y. Arii, B. Mikami, and M. Hirose Loop-inserted and thermostabilized structure of P1-P1′ cleaved ovalbumin mutant R339T J. Mol. Biol. 315 2002 113 120
    • (2002) J. Mol. Biol. , vol.315 , pp. 113-120
    • Yamasaki, M.1    Arii, Y.2    Mikami, B.3    Hirose, M.4
  • 18
    • 0037090807 scopus 로고    scopus 로고
    • Probing the serpin structural-transition mechanism in ovalbumin mutant R339T by proteolytic-cleavage kinetics of the reactive-centre loop
    • Y. Arii, and M. Hirose Probing the serpin structural-transition mechanism in ovalbumin mutant R339T by proteolytic-cleavage kinetics of the reactive-centre loop Biochem. J. 363 2002 403 409
    • (2002) Biochem. J. , vol.363 , pp. 403-409
    • Arii, Y.1    Hirose, M.2
  • 19
    • 0037046167 scopus 로고    scopus 로고
    • Probing the role of the F-helix in serpin stability through a single tryptophan substitution
    • L.D. Cabrita, J.C. Whisstock, and S.P. Bottomley Probing the role of the F-helix in serpin stability through a single tryptophan substitution Biochemistry 41 2002 4575 4581
    • (2002) Biochemistry , vol.41 , pp. 4575-4581
    • Cabrita, L.D.1    Whisstock, J.C.2    Bottomley, S.P.3
  • 20
    • 0037125184 scopus 로고    scopus 로고
    • The F-helix of serpins plays an essential, active role in the proteinase inhibition mechanism
    • P.G. Gettins The F-helix of serpins plays an essential, active role in the proteinase inhibition mechanism FEBS Letters 523 2002 2 6
    • (2002) FEBS Letters , vol.523 , pp. 2-6
    • Gettins, P.G.1
  • 21
    • 78651036085 scopus 로고
    • The transformation of ovalbumin into plakalbumin: A case of limited proteolysis
    • M. Ottesen The transformation of ovalbumin into plakalbumin: a case of limited proteolysis Compt. Rend. Trav. Lab. Carlsberg 30 1958 211 270
    • (1958) Compt. Rend. Trav. Lab. Carlsberg , vol.30 , pp. 211-270
    • Ottesen, M.1
  • 22
    • 0033160339 scopus 로고    scopus 로고
    • Conformational state of disulfide-reduced ovalbumin at acidic pH
    • E. Tatsumi, D. Yoshimatsu, and M. Hirose Conformational state of disulfide-reduced ovalbumin at acidic pH Biosci. Biotechnol. Biochem. 63 1999 1285 1290
    • (1999) Biosci. Biotechnol. Biochem. , vol.63 , pp. 1285-1290
    • Tatsumi, E.1    Yoshimatsu, D.2    Hirose, M.3
  • 23
    • 0028281746 scopus 로고
    • Engineering plasminogen activator inhibitor 1 mutants with increased functional stability
    • D.A. Lawrence, S.T. Olson, S. Palaniappan, and D. Ginsburg Engineering plasminogen activator inhibitor 1 mutants with increased functional stability Biochemistry 33 1994 3643 3648
    • (1994) Biochemistry , vol.33 , pp. 3643-3648
    • Lawrence, D.A.1    Olson, S.T.2    Palaniappan, S.3    Ginsburg, D.4
  • 24
    • 0035797920 scopus 로고    scopus 로고
    • Resolution of Michaelis complex, acylation, and conformational change steps in the reactions of the serpin, plasminogen activator inhibitor-1, with tissue plasminogen activator and trypsin
    • S.T. Olson, R. Swanson, D. Day, I. Verhamme, J. Kvassman, and J.D. Shore Resolution of Michaelis complex, acylation, and conformational change steps in the reactions of the serpin, plasminogen activator inhibitor-1, with tissue plasminogen activator and trypsin Biochemistry 40 2001 11742 11756
    • (2001) Biochemistry , vol.40 , pp. 11742-11756
    • Olson, S.T.1    Swanson, R.2    Day, D.3    Verhamme, I.4    Kvassman, J.5    Shore, J.D.6
  • 25
    • 0038053035 scopus 로고    scopus 로고
    • Serpin polymerization is prevented by a hydrogen bond network that is centered on His-334 and stabilized by glycerol
    • A. Zhou, P.E. Stein, J.A. Huntington, and R.W. Carrell Serpin polymerization is prevented by a hydrogen bond network that is centered on His-334 and stabilized by glycerol J. Biol. Chem. 278 2003 15116 15122
    • (2003) J. Biol. Chem. , vol.278 , pp. 15116-15122
    • Zhou, A.1    Stein, P.E.2    Huntington, J.A.3    Carrell, R.W.4
  • 26
    • 0030059689 scopus 로고    scopus 로고
    • Forces contributing to the conformational stability of proteins
    • C.N. Pace, B.A. Shirley, M. McNutt, and K. Gajiwala Forces contributing to the conformational stability of proteins FASEB J. 10 1996 75 83
    • (1996) FASEB J. , vol.10 , pp. 75-83
    • Pace, C.N.1    Shirley, B.A.2    McNutt, M.3    Gajiwala, K.4
  • 27
    • 0034608856 scopus 로고    scopus 로고
    • Regulation of protein function by native metastability
    • C. Lee, S.H. Park, M.Y. Lee, and M.H. Yu Regulation of protein function by native metastability Proc. Natl Acad. Sci. USA 97 2000 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
  • 29
    • 3342889562 scopus 로고    scopus 로고
    • Different conformational changes within the F-helix occur during serpin folding, polymerization, and proteinase inhibition
    • L.D. Cabrita, W. Dai, and S.P. Bottomley Different conformational changes within the F-helix occur during serpin folding, polymerization, and proteinase inhibition Biochemistry 43 2004 9834 9839
    • (2004) Biochemistry , vol.43 , pp. 9834-9839
    • Cabrita, L.D.1    Dai, W.2    Bottomley, S.P.3
  • 30
    • 0026736742 scopus 로고
    • Reversible denaturation of disulfide-reduced ovalbumin and its reoxidation generating the native cystine cross-link
    • N. Takahashi, and M. Hirose Reversible denaturation of disulfide-reduced ovalbumin and its reoxidation generating the native cystine cross-link J. Biol. Chem. 267 1992 11565 11572
    • (1992) J. Biol. Chem. , vol.267 , pp. 11565-11572
    • Takahashi, N.1    Hirose, M.2
  • 31
    • 0000629760 scopus 로고
    • The denaturation of proteins II. Ultraviolet absorption spectra of bovine serum albumin and ovalbumin in urea and in acid solution
    • A.N. Glazer, H.A. McKenzie, and R.G. Wake The denaturation of proteins II. Ultraviolet absorption spectra of bovine serum albumin and ovalbumin in urea and in acid solution Biochim. Biophys. Acta 69 1963 240 248
    • (1963) Biochim. Biophys. Acta , vol.69 , pp. 240-248
    • Glazer, A.N.1    McKenzie, H.A.2    Wake, R.G.3
  • 32
    • 0001243390 scopus 로고
    • A modified spectrophotometric determination of chymotrypsin, trypsin, and thrombin
    • B.C.W. Hummel A modified spectrophotometric determination of chymotrypsin, trypsin, and thrombin Can. J. Biochem. Physiol. 37 1959 1393 1399
    • (1959) Can. J. Biochem. Physiol. , vol.37 , pp. 1393-1399
    • Hummel, B.C.W.1
  • 33
    • 0041816077 scopus 로고    scopus 로고
    • Crystal structure of S-ovalbumin as a non-loop-inserted thermostabilized serpin form
    • M. Yamasaki, N. Takahashi, and M. Hirose Crystal structure of S-ovalbumin as a non-loop-inserted thermostabilized serpin form J. Biol. Chem. 278 2003 35524 35530
    • (2003) J. Biol. Chem. , vol.278 , pp. 35524-35530
    • Yamasaki, M.1    Takahashi, N.2    Hirose, M.3
  • 34
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • P.J. Kraulis 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
  • 35
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • E.A. Merritt, and D.J. Bacon Raster3D: photorealistic molecular graphics Methods Enzymol. 277 1997 505 524
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.