메뉴 건너뛰기




Volumn 288, Issue 44, 2013, Pages 32020-32035

Kinetic intermediates en route to the final serpin-protease complex: Studies of complexes of α1-protease inhibitor with Trypsin

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONAL CHANGE; DOCKING SITES; INTERMEDIATE STAGE; MICHAELIS COMPLEX; PROTEASE INHIBITOR; REACTIVE CENTER LOOPS; SITE-SPECIFIC; TRAPPING MECHANISMS;

EID: 84887033560     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.510990     Document Type: Article
Times cited : (15)

References (25)
  • 3
    • 0036882395 scopus 로고    scopus 로고
    • Serpin structure, mechanism, and function
    • Gettins, P. (2002) Serpin structure, mechanism, and function. Chem. Rev. 102, 4751-4804
    • (2002) Chem. Rev. , vol.102 , pp. 4751-4804
    • Gettins, P.1
  • 4
    • 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 β-sheet A
    • DOI 10.1073/pnas.96.9.4808
    • Stratikos, E., and Gettins, P. G. (1999) Formation of the covalent serpinproteinase complex involves translocation of the proteinase by more than 70 Å and full insertion of the reactive center loop into β-sheet A. Proc. Natl. Acad. Sci. U.S.A. 96, 4808-4813 (Pubitemid 29214493)
    • (1999) Proceedings of the National Academy of Sciences of the United States of America , vol.96 , Issue.9 , pp. 4808-4813
    • Stratikos, E.1    Gettins, P.G.W.2
  • 5
    • 0034687422 scopus 로고    scopus 로고
    • Structure of a serpin-protease complex shows inhibition by deformation
    • Huntington, J. A., and Read., R. J., and Carrell, R. W. (2000) Structure of a serpin-protease complex shows inhibition by deformation. Nature 407, 923-926
    • (2000) Nature , vol.407 , pp. 923-926
    • Huntington, J.A.1    Read, R.J.2    Carrell, R.W.3
  • 7
    • 0034601827 scopus 로고    scopus 로고
    • 15N HSQC NMR as a sensitive nonperturbing monitor of conformation
    • 15N HSQC NMR as a sensitive nonperturbing monitor of conformation. Biochemistry 39, 11884-11892
    • (2000) Biochemistry , vol.39 , pp. 11884-11892
    • Peterson, F.C.1    Gordon, N.C.2    Gettins, P.G.3
  • 8
    • 0035967508 scopus 로고    scopus 로고
    • 1-proteinase inhibitor pittsburgh-trypsin covalent complex
    • 1-proteinase inhibitor Pittsburgh-trypsin covalent complex. Biochemistry 40, 6284-6892
    • (2001) Biochemistry , vol.40 , pp. 6284-6892
    • Peterson, F.C.1    Gettins, P.G.2
  • 9
    • 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
    • DOI 10.1021/bi0107290
    • Olson, S. T., Swanson, R., Day, D., Verhamme, I., Kvassman, J., and Shore, J. D. (2001) Resolution of Michaelis complex, acylation and conformational change steps in the reactions of the serpin PAI-1 with trypsin and tissue plasminogen activator. Biochemistry 40, 11742-11756 (Pubitemid 32906036)
    • (2001) Biochemistry , vol.40 , Issue.39 , pp. 11742-11756
    • Olson, S.T.1    Swanson, R.2    Day, D.3    Verhamme, I.4    Kvassman, J.5    Shore, J.D.6
  • 10
    • 36348959744 scopus 로고    scopus 로고
    • Mechanism by which exosites promote the inhibition of blood coagulation proteases by heparin-activated antithrombin
    • DOI 10.1074/jbc.M702462200
    • Izaguirre, G., Swanson, R., Raja, S. M., and Rezaie., A. R., and Olson, S. T. (2007) Mechanism by which exosites promote the inhibition of blood coagulation proteases by heparin-activated antithrombin. J. Biol. Chem. 282, 33609-33622 (Pubitemid 350159518)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.46 , pp. 33609-33622
    • Izaguirre, G.1    Swanson, R.2    Raja, S.M.3    Rezaie, A.R.4    Olson, S.T.5
  • 11
    • 0035980118 scopus 로고    scopus 로고
    • The pH dependence of serpin-proteinase complex dissociation reveals a mechanism of complex stabilization involving inactive and active conformational states of the proteinase which are perturbable by calcium
    • Calugaru, S. V., Swanson, R., and Olson, S. T. (2001) The pH dependence of serpin-proteinase complex dissociation reveals a mechanism of complex stabilization involving inactive and active conformational states of the proteinase which are perturbable by calcium. J. Biol. Chem. 276, 32446-32455
    • (2001) J. Biol. Chem. , vol.276 , pp. 32446-32455
    • Calugaru, S.V.1    Swanson, R.2    Olson, S.T.3
  • 12
    • 0035815470 scopus 로고    scopus 로고
    • Intrinsic fluorescence changes and rapid kinetics of proteinase deformation during serpin inhibition
    • DOI 10.1016/S0014-5793(01)02305-5, PII S0014579301023055
    • Tew, D. J., and Bottomley, S. P. (2001) Intrinsic fluorescence changes and rapid kinetics of proteinase deformation during serpin inhibition. FEBS Lett. 494, 30-33 (Pubitemid 32289366)
    • (2001) FEBS Letters , vol.494 , Issue.1-2 , pp. 30-33
    • Tew, D.J.1    Bottomley, S.P.2
  • 13
    • 0348111457 scopus 로고    scopus 로고
    • Distortion of the Catalytic Domain of Tissue-type Plasminogen Activator by Plasminogen Activator Inhibitor-1 Coincides with the Formation of Stable Serpin-Proteinase Complexes
    • DOI 10.1074/jbc.M306184200
    • Perron, M. J., and Blouse., G. E., and Shore, J. D. (2003) Distortion of the catalytic domain of tissue-type plasminogen activator by plasminogen activator inhibitor-1 coincides with the formation of stable serpin-proteinase complexes. J. Biol. Chem. 278, 48197-48203 (Pubitemid 37523273)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.48 , pp. 48197-48203
    • Perron, M.J.1    Blouse, G.E.2    Shore, J.D.3
  • 15
    • 0037125184 scopus 로고    scopus 로고
    • The F-helix of serpins plays an essential, active role in the proteinase inhibition mechanism
    • DOI 10.1016/S0014-5793(02)02924-1, PII S0014579302029241
    • Gettins, P. G. (2002) The F-helix of serpins plays an essential, active role in the proteinase inhibition mechanism. FEBS Lett. 523, 2-6 (Pubitemid 34786048)
    • (2002) FEBS Letters , vol.523 , Issue.1-3 , pp. 2-6
    • Gettins, P.G.W.1
  • 17
    • 59449098023 scopus 로고    scopus 로고
    • Engineering functional antithrombin exosites in α1-proteinase inhibitor that specifically enhance the inhibiiton of factor xa and factor IXa
    • Izaguirre, G., and Rezaie., A. R., and Olson, S. T. (2009) Engineering functional antithrombin exosites in α1-proteinase inhibitor that specifically enhance the inhibiiton of factor Xa and factor IXa. J. Biol. Chem. 284, 1550-1558
    • (2009) J. Biol. Chem. , vol.284 , pp. 1550-1558
    • Izaguirre, G.1    Rezaie, A.R.2    Olson, S.T.3
  • 19
    • 0029587003 scopus 로고
    • Role of the catalytic serine in the interactions of serine proteinases with protein inhibitors of the serpin family. Contribution of a covalent interaction to the binding energy of serpin-proteinase complexes
    • Olson, S. T., and Bock., P. E., Kvassman, J., Shore, J. D., and Lawrence., D. A., Ginsburg, D., and Björk, I. (1995) Role of the catalytic serine in the interactions of serine proteinases with protein inhibitors of the serpin family. Contribution of a covalent interaction to the binding energy of serpin-proteinase complexes. J. Biol. Chem. 270, 30007-30017
    • (1995) J. Biol. Chem. , vol.270 , pp. 30007-30017
    • Olson, S.T.1    Bock, P.E.2    Kvassman, J.3    Shore, J.D.4    Lawrence, D.A.5    Ginsburg, D.6    Björk, I.7
  • 20
    • 34047254892 scopus 로고    scopus 로고
    • Serine and cysteine proteases are translocated to similar extents upon formation of covalent complexes with serpins
    • Swanson, R., and Raghavendra., M. P., Zhang, W., Froelich, C, and Gettins., P. G., and Olson, S. T. (2007) Serine and cysteine proteases are translocated to similar extents upon formation of covalent complexes with serpins. J. Biol. Chem. 282, 2305-2313
    • (2007) J. Biol. Chem. , vol.282 , pp. 2305-2313
    • Swanson, R.1    Raghavendra, M.P.2    Zhang, W.3    Froelich, C.4    Gettins, P.G.5    Olson, S.T.6
  • 21
    • 0025833143 scopus 로고
    • Papain labelled with fluorescent thiol-specific reagents as a probe for characterization of interactions between cysteine proteinases and their protein inhibitors by competitive titrations
    • Lindahl, P., Raub-Segall, E., Olson, S. T., and Björk, I. (1991) Papain labelled with fluorescent thiol-specific reagents as a probe for characterization of interactions between cysteine proteinases and their protein inhibitors by competitive titrations. Biochem. J. 276, 387-394
    • (1991) Biochem. J. , vol.276 , pp. 387-394
    • Lindahl, P.1    Raub-Segall, E.2    Olson, S.T.3    Björk, I.4
  • 24
    • 33644859395 scopus 로고    scopus 로고
    • Active-site distortion is sufficient for proteinase inhibition by serpins
    • Dementiev, A., Dobó, J., and Gettins, P. G. (2006) Active-site distortion is sufficient for proteinase inhibition by serpins. J. Biol. Chem. 281, 3452-3457
    • (2006) J. Biol. Chem. , vol.281 , pp. 3452-3457
    • Dementiev, A.1    Dobó, J.2    Gettins, P.G.3
  • 25
    • 0032558454 scopus 로고    scopus 로고
    • Change in environment of the P1 side chain upon progression from the Michaelis complex to the covalent serpin - Proteinase complex
    • DOI 10.1021/bi981234m
    • Futamura, A., Stratikos, E., Olson, S. T., and Gettins, P. G. (1998) Change in environment of the P1 side chain upon progression from the Michaelis complex to the covalent serpin-proteinase complex. Biochemistry 37, 13110-13119 (Pubitemid 28449554)
    • (1998) Biochemistry , vol.37 , Issue.38 , pp. 13110-13119
    • Futamura, A.1    Stratikos, E.2    Olson, S.T.3    Gettins, P.G.W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.