메뉴 건너뛰기




Volumn 5, Issue 5, 1996, Pages 825-835

Comparison of the structures of the cyclotheonamide A complexes of human α-thrombin and bovine β-trypsin

Author keywords

cyclotheonamide A; thrombin; transition state analogue; trypsin; keto amide

Indexed keywords

CYCLOTHEONAMIDE A; PENTAPEPTIDE; THROMBIN; TRYPSIN; UNCLASSIFIED DRUG;

EID: 0029985841     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560050504     Document Type: Article
Times cited : (39)

References (53)
  • 1
    • 0025035782 scopus 로고
    • Substrate specificity for the human rotamase FKBP: A view of FK506 and rapamycin as leucine-(twisted amide)-proline mimics
    • Albers MW, Walsh CT, Schreiber SL. 1990. Substrate specificity for the human rotamase FKBP: A view of FK506 and rapamycin as leucine-(twisted amide)-proline mimics. J Org Chem 55:4984-4986.
    • (1990) J Org Chem , vol.55 , pp. 4984-4986
    • Albers, M.W.1    Walsh, C.T.2    Schreiber, S.L.3
  • 2
    • 0025328906 scopus 로고
    • Highly active and selective anticoagulants: D-Phe-Pro-Arg-H, a free tripeptide aldehyde prone to spontaneous inactivation, and its stable N-methyl derivative, D-Me-Phe-Pro-Arg-H
    • Bajusz S, Szell E, Bagdy D, Barabas E, Horvath G, Dioszegi M, Fittler Z, Szabo G, Juhasz A, Tomori E, Szilagyi G. 1990. Highly active and selective anticoagulants: D-Phe-Pro-Arg-H, a free tripeptide aldehyde prone to spontaneous inactivation, and its stable N-methyl derivative, D-Me-Phe-Pro-Arg-H. J Mol Chem 33:1729-1735.
    • (1990) J Mol Chem , vol.33 , pp. 1729-1735
    • Bajusz, S.1    Szell, E.2    Bagdy, D.3    Barabas, E.4    Horvath, G.5    Dioszegi, M.6    Fittler, Z.7    Szabo, G.8    Juhasz, A.9    Tomori, E.10    Szilagyi, G.11
  • 4
    • 0024791521 scopus 로고
    • Crystal structure of bovine β-trypsin at 1.5 Å resolution in a crystal form with low molecular packing density
    • Bartunik HD, Summers LJ, Bartsch HH. 1989. Crystal structure of bovine β-trypsin at 1.5 Å resolution in a crystal form with low molecular packing density. J Mol Biol 210:813-828.
    • (1989) J Mol Biol , vol.210 , pp. 813-828
    • Bartunik, H.D.1    Summers, L.J.2    Bartsch, H.H.3
  • 5
    • 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
  • 6
    • 0025175641 scopus 로고
    • α2-naphthyl-sulphonyl-giycyl-DL-p-arnidinophenylalanyl- piperidine (NAPAP) and (2R,4R)-4-methyl-1-[N-(3-methyl-1,2,3,4-tetrahydro-8-quinolinesulphonyl)-L- arginyl]-2-piperidine carboxylic acid (MQPA) to human α-thrombin
    • α2-naphthyl-sulphonyl-giycyl)-DL-p-arnidinophenylalanyl- piperidine (NAPAP) and (2R,4R)-4-methyl-1-[N-(3-methyl-1,2,3,4-tetrahydro-8-quinolinesulphonyl)-L- arginyl]-2-piperidine carboxylic acid (MQPA) to human α-thrombin. Eur J Biochem 93:175-182.
    • (1990) Eur J Biochem , vol.93 , pp. 175-182
    • Bode, W.1    Turk, D.2    Sturzebecher, J.3
  • 7
    • 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
  • 8
    • 84944812221 scopus 로고
    • Extension of molecular replacement: A new search strategy based on Patterson correlation refinement
    • Brunger AT. 1990. Extension of molecular replacement: A new search strategy based on Patterson correlation refinement. Acta Crystallogr A 46:46.
    • (1990) Acta Crystallogr A , vol.46 , pp. 46
    • Brunger, A.T.1
  • 10
    • 84901961522 scopus 로고
    • Slow-cooling protocols for crystallographic refinement
    • Brunger AT, Krukowski A, Erickson J. 1990. Slow-cooling protocols for crystallographic refinement. Acta Crystallogr A 46:585-593.
    • (1990) Acta Crystallogr A , vol.46 , pp. 585-593
    • Brunger, A.T.1    Krukowski, A.2    Erickson, J.3
  • 11
    • 0025674180 scopus 로고
    • Bifunctional thrombin inhibitors based on the sequence of hirudin
    • DiMaio J, Gibbs B, Munn D, Lefebre J, Ni F, Konishi Y. 1990. Bifunctional thrombin inhibitors based on the sequence of hirudin. J Biol Chem 265: 21698-21703.
    • (1990) J Biol Chem , vol.265 , pp. 21698-21703
    • DiMaio, J.1    Gibbs, B.2    Munn, D.3    Lefebre, J.4    Ni, F.5    Konishi, Y.6
  • 12
    • 0023684353 scopus 로고
    • Regulation of thrombin generation and functions
    • Fenton JW II. 1988a. Regulation of thrombin generation and functions. Semin Thromb Hemost 14:234-240.
    • (1988) Semin Thromb Hemost , vol.14 , pp. 234-240
    • Fenton II, J.W.1
  • 13
    • 0001061599 scopus 로고
    • Thrombin bioregulatory functions
    • Fenton JW II. 1988b. Thrombin bioregulatory functions. Adv Clin Enzymol 6:186-193.
    • (1988) Adv Clin Enzymol , vol.6 , pp. 186-193
    • Fenton II, J.W.1
  • 14
    • 0002301187 scopus 로고
    • Incorporation of fast Fourier transforms to speed restrained least-squares refinement of protein structures
    • Finzel BC. 1987. Incorporation of fast Fourier transforms to speed restrained least-squares refinement of protein structures. J Appl Crystallogr 20: 53-55.
    • (1987) J Appl Crystallogr , vol.20 , pp. 53-55
    • Finzel, B.C.1
  • 15
    • 0024992889 scopus 로고
    • Cyclotheonamides, potent thrombin inhibitors, from a marine sponge Theonella sp.
    • Fusetani N, Matsunaga S, Matsumoto H, Takebayashi Y. 1990. Cyclotheonamides, potent thrombin inhibitors, from a marine sponge Theonella sp. J Am Chem Soc 112:7053-7054.
    • (1990) J Am Chem Soc , vol.112 , pp. 7053-7054
    • Fusetani, N.1    Matsunaga, S.2    Matsumoto, H.3    Takebayashi, Y.4
  • 16
    • 5244277903 scopus 로고
    • Purification of thrombin and isolation of a peptide containing the active center histidine
    • Glover G, Shaw E. 1971. Purification of thrombin and isolation of a peptide containing the active center histidine. J Biol Chem 246:4594-4601.
    • (1971) J Biol Chem , vol.246 , pp. 4594-4601
    • Glover, G.1    Shaw, E.2
  • 17
    • 0026795414 scopus 로고
    • Reassignment of stereochemistry and total synthesis of the thrombin inhibitor cyclotheonamide B
    • Haghihara M, Schreiber SL. 1992. Reassignment of stereochemistry and total synthesis of the thrombin inhibitor cyclotheonamide B. J Am Chem Soc 114:6570-6571.
    • (1992) J Am Chem Soc , vol.114 , pp. 6570-6571
    • Haghihara, M.1    Schreiber, S.L.2
  • 19
    • 0002595956 scopus 로고
    • Stereochemically restrained crystallographic least-squares refinement of macromolecular structures
    • Srinivasan R, ed. Oxford: Pergamon Press
    • Hendrickson WA, Konnert JH. 1980. Stereochemically restrained crystallographic least-squares refinement of macromolecular structures. In: Srinivasan R, ed. Biomolecular structure, function, conformation and evolution. Oxford: Pergamon Press, pp 43-57.
    • (1980) Biomolecular Structure, Function, Conformation and Evolution , pp. 43-57
    • Hendrickson, W.A.1    Konnert, J.H.2
  • 20
    • 0001008852 scopus 로고
    • Auto-indexing of oscillation images
    • Higashi T. 1990. Auto-indexing of oscillation images. J Appl Crystallogr 23:253-257.
    • (1990) J Appl Crystallogr , vol.23 , pp. 253-257
    • Higashi, T.1
  • 21
    • 0022326269 scopus 로고
    • Software for a diffractometer with multiwire area detector
    • Howard AD, Nielson C, Xuong NH. 1985. Software for a diffractometer with multiwire area detector. Methods Enzymol 114:452-472.
    • (1985) Methods Enzymol , vol.114 , pp. 452-472
    • Howard, A.D.1    Nielson, C.2    Xuong, N.H.3
  • 22
    • 0025102977 scopus 로고
    • Inhibition of cathepsin B and papain by peptidyl α-keto esters, α-ketoamides, α-diketones and α-ketoacids
    • Hu LY, Abeles RH. 1990. Inhibition of cathepsin B and papain by peptidyl α-keto esters, α-ketoamides, α-diketones and α-ketoacids. Arch Biochem Biophys 281:271-274.
    • (1990) Arch Biochem Biophys , vol.281 , pp. 271-274
    • Hu, L.Y.1    Abeles, R.H.2
  • 23
    • 33947092515 scopus 로고
    • Structural basis of the activation and activation of trypsin
    • Huber R, Bode W. 1978. Structural basis of the activation and activation of trypsin. Acc Chem Res 11:114-122.
    • (1978) Acc Chem Res , vol.11 , pp. 114-122
    • Huber, R.1    Bode, W.2
  • 24
    • 0025952925 scopus 로고
    • HIV protease: A novel chemotherapeutic target for AIDS
    • Huff JR. 1991. HIV protease: A novel chemotherapeutic target for AIDS. J Med Chem 34:2305-2314.
    • (1991) J Med Chem , vol.34 , pp. 2305-2314
    • Huff, J.R.1
  • 25
    • 0000356656 scopus 로고
    • A graphics model building and refinement system for macromolecules
    • Jones TA. 1978. A graphics model building and refinement system for macromolecules. J Appl Crystallogr 11:268-272.
    • (1978) J Appl Crystallogr , vol.11 , pp. 268-272
    • Jones, T.A.1
  • 26
    • 0018750813 scopus 로고
    • D-Phe-Pro-Arg CH Cl - A selective affinity label for thrombin
    • Kettner C, Shaw E. 1979 D-Phe-Pro-Arg CH Cl - A selective affinity label for thrombin. Thromb Res 14:969-973.
    • (1979) Thromb Res , vol.14 , pp. 969-973
    • Kettner, C.1    Shaw, E.2
  • 27
    • 0019750662 scopus 로고
    • Inactivation of trypsin-like enzymes with peptides of arginine chloromethyl ketone
    • Kettner C, Shaw E. 1981. Inactivation of trypsin-like enzymes with peptides of arginine chloromethyl ketone. Methods Enzymol 80:826-848.
    • (1981) Methods Enzymol , vol.80 , pp. 826-848
    • Kettner, C.1    Shaw, E.2
  • 29
    • 0021327417 scopus 로고
    • Selective inhibition of thrombin by (2R, 4R)-4-methyl-1-(N2-[(3-methyl-1,2,3,4-tetrahydro-8-quinolinyl)sulpho nyl)-L-arginyl]-2-piperidine-carboxylic acid
    • Kikumoto R, Tamao Y, Tezuka T, Tonomura S, Hara H, Ninomiya K, Hijikata A, Okamoto S. 1984. Selective inhibition of thrombin by (2R, 4R)-4-methyl-1-(N2-[(3-methyl-1,2,3,4-tetrahydro-8-quinolinyl)sulpho nyl)-L-arginyl)]-2-piperidine-carboxylic acid. Biochemistry 23:85-90.
    • (1984) Biochemistry , vol.23 , pp. 85-90
    • Kikumoto, R.1    Tamao, Y.2    Tezuka, T.3    Tonomura, S.4    Hara, H.5    Ninomiya, K.6    Hijikata, A.7    Okamoto, S.8
  • 30
    • 0022335493 scopus 로고
    • Use of the rotation and translation function
    • Lattman E. 1985. Use of the rotation and translation function. Methods Enzymol 115.55.
    • (1985) Methods Enzymol , vol.115 , pp. 55
    • Lattman, E.1
  • 31
    • 15844387909 scopus 로고
    • Structure of the trypsin-cyclotheonamide a complex: An all-natural approach
    • Lee AY, Clardy J. 1994. Structure of the trypsin-cyclotheonamide A complex: An all-natural approach. Chem Biol (Introductory issue):10-11.
    • (1994) Chem Biol , Issue.INTRODUCTORY ISSUE , pp. 10-11
    • Lee, A.Y.1    Clardy, J.2
  • 32
    • 0027849639 scopus 로고
    • Atomic structure of the trypsin-cyclotheonamide A complex: Lessons for the design of serine protease inhibitors
    • Lee AY, Hagihara M, Karmacharya R, Albers MW, Schreiber SL, Clardy J. 1993. Atomic structure of the trypsin-cyclotheonamide A complex: Lessons for the design of serine protease inhibitors. J Am Chem Soc 115:12619-12620.
    • (1993) J Am Chem Soc , vol.115 , pp. 12619-12620
    • Lee, A.Y.1    Hagihara, M.2    Karmacharya, R.3    Albers, M.W.4    Schreiber, S.L.5    Clardy, J.6
  • 33
  • 34
    • 0001099937 scopus 로고
    • Traitement statistique des erreuis dans la determination des structures cristallines
    • Luzzati V. 1952 Traitement statistique des erreuis dans la determination des structures cristallines. Acta Crystallogr 5:802-810
    • (1952) Acta Crystallogr , vol.5 , pp. 802-810
    • Luzzati, V.1
  • 37
    • 0018374004 scopus 로고
    • Interactions of a fluorescent active-site-directed inhibitor of thrombin: Dansylarginine N-(3-ethyl-1,5-pentanediyl) amide
    • Nesheim ME, Prendergast FG, Mann KG. 1979. Interactions of a fluorescent active-site-directed inhibitor of thrombin: Dansylarginine N-(3-ethyl-1,5-pentanediyl) amide. Biochemistry 18.996-1003
    • (1979) Biochemistry , vol.18 , pp. 996-1003
    • Nesheim, M.E.1    Prendergast, F.G.2    Mann, K.G.3
  • 38
    • 0026563021 scopus 로고
    • Keto amide inhibitors of aminopeptidases
    • Ocain TD, Rich DH. 1992 Keto amide inhibitors of aminopeptidases. J Med Chem 35.451-456.
    • (1992) J Med Chem , vol.35 , pp. 451-456
    • Ocain, T.D.1    Rich, D.H.2
  • 39
    • 0025176920 scopus 로고
    • Synthesis of peptidyl fluoromethyl ketones and peptidyl α-keto esters as inhibitors of porcine pancreatic elastase, human neutrophil elastase, and rat and human neutrophtl cathepsin G
    • Peet NP, Burkhart JP, Angelastro MR, Giroux EL, Mehdi S, Bey P. Kolb M, Neises B, Schirlin D 1990. Synthesis of peptidyl fluoromethyl ketones and peptidyl α-keto esters as inhibitors of porcine pancreatic elastase, human neutrophil elastase, and rat and human neutrophtl cathepsin G. J Med Chem 33:394-407.
    • (1990) J Med Chem , vol.33 , pp. 394-407
    • Peet, N.P.1    Burkhart, J.P.2    Angelastro, M.R.3    Giroux, E.L.4    Mehdi, S.5    Bey, P.6    Kolb, M.7    Neises, B.8    Schirlin, D.9
  • 40
  • 41
    • 0025302066 scopus 로고
    • Inhibition of FKBP rotamase activity by immunosuppressant FK506: Twisted amide surrogate
    • Rosen MK, Standaert RF, Galat A, Nakatsuka M, Schreiber SL. 1990. Inhibition of FKBP rotamase activity by immunosuppressant FK506: Twisted amide surrogate. Science 248:863-866.
    • (1990) Science , vol.248 , pp. 863-866
    • Rosen, M.K.1    Standaert, R.F.2    Galat, A.3    Nakatsuka, M.4    Schreiber, S.L.5
  • 42
    • 0002660809 scopus 로고
    • The detection of sub-units within the crystallographic asymmetric unit
    • Rossmann MG, Blou DM. 1962. The detection of sub-units within the crystallographic asymmetric unit. Acta Crystallogr 15:24-31.
    • (1962) Acta Crystallogr , vol.15 , pp. 24-31
    • Rossmann, M.G.1    Blou, D.M.2
  • 43
    • 0025866812 scopus 로고
    • Refined structure of hirudin-thrombin complex
    • Rydel TJ, Tulinsky A, Bode W, Huber R. 1991. Refined structure of hirudin-thrombin complex. J Mol Biol 221:277-280.
    • (1991) J Mol Biol , vol.221 , pp. 277-280
    • Rydel, T.J.1    Tulinsky, A.2    Bode, W.3    Huber, R.4
  • 44
    • 0000082544 scopus 로고
    • CHAIN - A crystallographic modelling program
    • Sack JS. 1988. CHAIN - A crystallographic modelling program. J Mol Graph 6:224-225.
    • (1988) J Mol Graph , vol.6 , pp. 224-225
    • Sack, J.S.1
  • 47
    • 0027409404 scopus 로고
    • A player of many parts: The spotlight falls on thrombin's structure
    • Stubba 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
    • Stubba, M.T.1    Bode, W.2
  • 48
    • 0027410184 scopus 로고
    • Active site and exosite binding of α-thrombin
    • Tulinsky A, Qiu X. 1993. Active site and exosite binding of α-thrombin. Blood Coagul Fibrinolysis 4:305-312.
    • (1993) Blood Coagul Fibrinolysis , vol.4 , pp. 305-312
    • Tulinsky, A.1    Qiu, X.2
  • 50
  • 51
    • 0028586082 scopus 로고
    • The structure of prethrombin-2: Changes accompanying activation and exosite binding 10 thrombin
    • Vijayalalshmi J, Padmanabhan KP, Mann KG, Tulinsky A. 1994 The structure of prethrombin-2: Changes accompanying activation and exosite binding 10 thrombin. Protein Sci 3:2254-2271.
    • (1994) Protein Sci , vol.3 , pp. 2254-2271
    • Vijayalalshmi, J.1    Padmanabhan, K.P.2    Mann, K.G.3    Tulinsky, A.4
  • 52
    • 0000134034 scopus 로고
    • Strategy for data collection from protein crystals using a multiwire counter area detector diffractometer
    • Xuong NH, Nielsen C, Hamlin R, Anderson D. 1985. Strategy for data collection from protein crystals using a multiwire counter area detector diffractometer. J Appl Crystallogr 18:342-350.
    • (1985) J Appl Crystallogr , vol.18 , pp. 342-350
    • Xuong, N.H.1    Nielsen, C.2    Hamlin, R.3    Anderson, D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.