메뉴 건너뛰기




Volumn 8, Issue 1, 1999, Pages 91-95

The crystal structure of α-thrombin-hirunorm IV complex reveals a novel specificity site recognition mode

Author keywords

Bifunctional synthetic thrombin inhibitors; Crystal structure; Hirunorms; Retro binding peptides

Indexed keywords

ARGININE; FIBRINOGEN; GLYCINE; HIRUDIN DERIVATIVE; HIRUNORM IV; SERINE; THROMBIN; TRIPEPTIDE; UNCLASSIFIED DRUG;

EID: 0032946325     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.8.1.91     Document Type: Article
Times cited : (10)

References (32)
  • 1
    • 0030847766 scopus 로고    scopus 로고
    • Protein data bank archives of three-dimensional macromolecular structures
    • Abola EE, Sussman JL, Prilusky J, Manning NO. 1997. Protein data bank archives of three-dimensional macromolecular structures. Methods Enzymol 277:556-571.
    • (1997) Methods Enzymol , vol.277 , pp. 556-571
    • Abola, E.E.1    Sussman, J.L.2    Prilusky, J.3    Manning, N.O.4
  • 2
    • 0028821302 scopus 로고
    • Proteinase inhibitors from the European medicinal leech Hirudo medicinalis: Structural functional and biomedical aspects
    • Ascenzi P, Amiconi G, Bode W, Bolognesi M, Coletta M, Menegatti E. 1995. Proteinase inhibitors from the European medicinal leech Hirudo medicinalis: Structural functional and biomedical aspects. Molec Aspects Med 16:215-313.
    • (1995) Molec Aspects Med , vol.16 , pp. 215-313
    • Ascenzi, P.1    Amiconi, G.2    Bode, W.3    Bolognesi, M.4    Coletta, M.5    Menegatti, E.6
  • 3
    • 0024431034 scopus 로고
    • The refined 1.9 Å crystal structure of human α-thrombin: Interaction with D-Phe-Pro-Arg-chloromethylketone and significance of the Tyr-Pro-Pro-Trp insertion segment
    • Bode W, Mayr I, Baumann U, Huber R, Stone SR, Hofsteenge J. 1989. The refined 1.9 Å crystal structure of human α-thrombin: Interaction with D-Phe-Pro-Arg-chloromethylketone and significance of the Tyr-Pro-Pro-Trp insertion segment. EMBO J 8:3467-3475.
    • (1989) EMBO J , vol.8 , pp. 3467-3475
    • Bode, W.1    Mayr, I.2    Baumann, U.3    Huber, R.4    Stone, S.R.5    Hofsteenge, J.6
  • 4
    • 0027050807 scopus 로고
    • The refined 1.9 Å X-ray crystal structure of D-Phe-Pro-Arg chloromethylketone-inhibited human α-thrombin: Structure analysis overall structure electrostatic properties detailed active-site geometry and structure-function relationships
    • Bode W, Turk D, Karshikov A. 1992. The refined 1.9 Å X-ray crystal structure of D-Phe-Pro-Arg chloromethylketone-inhibited human α-thrombin: Structure analysis overall structure electrostatic properties detailed active-site geometry and structure-function relationships. Protein Sci 1:426-471.
    • (1992) Protein Sci , vol.1 , pp. 426-471
    • Bode, W.1    Turk, D.2    Karshikov, A.3
  • 5
    • 0026465007 scopus 로고
    • Refined 2.3 Å X-ray crystal structure of bovine thrombin complexes formed with the benzamidine and arginine-based thrombin inhibitors NAPAP 4-TAPAP and MQPA
    • Brandstetter H, Turk D, Hoeffken HW, Grosse D, Stürzebecher J, Martin PD, Ewards BFP, Bode W. 1992. Refined 2.3 Å X-ray crystal structure of bovine thrombin complexes formed with the benzamidine and arginine-based thrombin inhibitors NAPAP 4-TAPAP and MQPA. J Mol Biol 226:1085-1099.
    • (1992) J Mol Biol , vol.226 , pp. 1085-1099
    • Brandstetter, H.1    Turk, D.2    Hoeffken, H.W.3    Grosse, D.4    Stürzebecher, J.5    Martin, P.D.6    Ewards, B.F.P.7    Bode, W.8
  • 6
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • 1994. The CCP4 suite: Programs for protein crystallography. Acta Crystallogr D50:760-767.
    • (1994) Acta Crystallogr , vol.D50 , pp. 760-767
  • 9
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • Engh RA, Huber R. 1991. Accurate bond and angle parameters for X-ray protein structure refinement. Acta Crystallogr A47:392-400.
    • (1991) Acta Crystallogr , vol.A47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 10
    • 0019729451 scopus 로고
    • Thrombin specificity
    • Fenton JW II. 1988. Thrombin specificity. Ann NY Acad Sci 370:468-495.
    • (1988) Ann NY Acad Sci , vol.370 , pp. 468-495
    • Fenton J.W. II1
  • 12
    • 0029896898 scopus 로고    scopus 로고
    • Crystal structure of two new bifunctional nonsubstrate type thrombin inhibitors complexed with human α-thrombin
    • Féthière J, Tsuda Y, Coulombe R, Konishi Y, Cygler M. 1996. Crystal structure of two new bifunctional nonsubstrate type thrombin inhibitors complexed with human α-thrombin. Protein Sci 5:1174-1183.
    • (1996) Protein Sci , vol.5 , pp. 1174-1183
    • Féthière, J.1    Tsuda, Y.2    Coulombe, R.3    Konishi, Y.4    Cygler, M.5
  • 14
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and location of errors in these models
    • Jones TA, Zou J-Y, Cowan S, Kieldgaard M. 1991. Improved methods for building protein models in electron density maps and location of errors in these models. Acta Crystallogr A47:110-119.
    • (1991) Acta Crystallogr , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.3    Kieldgaard, M.4
  • 16
    • 0029984910 scopus 로고    scopus 로고
    • Rational design of true hirudin mimetics: Synthesis and characterization of multisite directed α-thrombin inhibitors
    • Lombardi A, Nastri F, Della Morte R, Rossi A, De Rosa A, Staiano N, Pedone C, Pavone V. 1996. Rational design of true hirudin mimetics: Synthesis and characterization of multisite directed α-thrombin inhibitors. J Med Chem 39:2008-2017.
    • (1996) J Med Chem , vol.39 , pp. 2008-2017
    • Lombardi, A.1    Nastri, F.2    Della Morte, R.3    Rossi, A.4    De Rosa, A.5    Staiano, N.6    Pedone, C.7    Pavone, V.8
  • 17
    • 0027968823 scopus 로고
    • The development of hirudin as an antithrombotic drug
    • Markwardt F. 1994. The development of hirudin as an antithrombotic drug. Thrombosis Res 74:1-23.
    • (1994) Thrombosis Res , vol.74 , pp. 1-23
    • Markwardt, F.1
  • 18
    • 0029895694 scopus 로고    scopus 로고
    • A noncleavable retrobinding peptide that spans the substrate binding cleft of serine proteases. Atomic structure of nazumamide a: Human thrombin
    • Nienaber VL, Amparo EC. 1996. A noncleavable retrobinding peptide that spans the substrate binding cleft of serine proteases. Atomic structure of nazumamide A: Human thrombin. J Am Chem Soc 118:6807-6810.
    • (1996) J Am Chem Soc , vol.118 , pp. 6807-6810
    • Nienaber, V.L.1    Amparo, E.C.2
  • 19
    • 0031664267 scopus 로고    scopus 로고
    • Multiple binding mode of reversible synthetic thrombin inhibitors. A comparative structural analysis
    • Pavone V, De Simone G, Nastri F, Galdiero S, Staiano N, Lombardi A, Pedone C. 1998. Multiple binding mode of reversible synthetic thrombin inhibitors. A comparative structural analysis. Biol Chem 379:987-1006.
    • (1998) Biol Chem , vol.379 , pp. 987-1006
    • Pavone, V.1    De Simone, G.2    Nastri, F.3    Galdiero, S.4    Staiano, N.5    Lombardi, A.6    Pedone, C.7
  • 21
    • 0025866812 scopus 로고
    • Refined structure of the hirudin-thrombin complex
    • Rydel TJ, Tulinsky A, Bode W, Huber R. 1991. Refined structure of the hirudin-thrombin complex. J Mol Biol 221:583-601.
    • (1991) J Mol Biol , vol.221 , pp. 583-601
    • Rydel, T.J.1    Tulinsky, A.2    Bode, W.3    Huber, R.4
  • 22
    • 0014211618 scopus 로고
    • On the size of the active-site in proteinases I papain
    • Schechter I, Berger A. 1967. On the size of the active-site in proteinases I Papain. Biochem Biophys Res Commun 27:157-162.
    • (1967) Biochem Biophys Res Commun , vol.27 , pp. 157-162
    • Schechter, I.1    Berger, A.2
  • 26
    • 0027409404 scopus 로고
    • A player of many parts: The spotlight falls on thrombin's structure
    • Stubbs MT, Bode W. 1993. A player of many parts: The spotlight falls on thrombin's structure. Thromb Res 69:1-58.
    • (1993) Thromb Res , vol.69 , pp. 1-58
    • Stubbs, M.T.1    Bode, W.2
  • 27
    • 0029083512 scopus 로고
    • Structure and specificity in coagulation and its inhibition
    • Stubbs MT, Bode W. 1995. Structure and specificity in coagulation and its inhibition. Trends Cardiovasc Med 5:157-166.
    • (1995) Trends Cardiovasc Med , vol.5 , pp. 157-166
    • Stubbs, M.T.1    Bode, W.2
  • 29
    • 0027427161 scopus 로고
    • Synthetic low molecular weight thrombin inhibitors: Molecular design and pharmacological profile
    • Tapparelli C, Metternich R, Ehrhardt C, Cook NS. 1993. Synthetic low molecular weight thrombin inhibitors: Molecular design and pharmacological profile. Trends Pharmacol Sci 14:366-376.
    • (1993) Trends Pharmacol Sci , vol.14 , pp. 366-376
    • Tapparelli, C.1    Metternich, R.2    Ehrhardt, C.3    Cook, N.S.4
  • 30
    • 84913050729 scopus 로고
    • An efficient general purpose least squares refinement program for macromolecular structures
    • Tronrud D, TenEyck LF, Matthews BW. 1987. An efficient general purpose least squares refinement program for macromolecular structures. Acta Crystallogr A34:489-501.
    • (1987) Acta Crystallogr , vol.A34 , pp. 489-501
    • Tronrud, D.1    TenEyck, L.F.2    Matthews, B.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.