메뉴 건너뛰기




Volumn 7, Issue 6, 1998, Pages 1303-1309

Structure of malonic acid-based inhibitors bound to human neutrophil collagenase. A new binding mode explains apparently anomalous data

Author keywords

Binding mode; Drug design; Inhibitor; Malonic acid; Matrix metalloproteinase; MMP 8

Indexed keywords

COLLAGENASE INHIBITOR; HYDROXAMIC ACID; MALONIC ACID DERIVATIVE; MATRIX METALLOPROTEINASE; MATRIX METALLOPROTEINASE INHIBITOR; NEUTROPHIL COLLAGENASE; PHOSPHINIC ACID DERIVATIVE; THIOL DERIVATIVE;

EID: 0031798691     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560070605     Document Type: Article
Times cited : (49)

References (27)
  • 4
    • 0029055072 scopus 로고
    • Hydroxamic acids as potent inhibitors of endothelin-converting enzyme from human bronchiolar smooth muscle
    • Bihovsky R, Levinson BL, Loewi RC, Erhardt PW, Polokoff MAJ. 1995. Hydroxamic acids as potent inhibitors of endothelin-converting enzyme from human bronchiolar smooth muscle. Med Chem 38:2119-2129.
    • (1995) Med Chem , vol.38 , pp. 2119-2129
    • Bihovsky, R.1    Levinson, B.L.2    Loewi, R.C.3    Erhardt, P.W.4    Polokoff, M.A.J.5
  • 5
    • 0027515396 scopus 로고
    • Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the "metzincins."
    • Bode W, Gomis-Rüth F-X, Stöcker W. 1993. Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the "metzincins." FEBS Lett 331:134-140.
    • (1993) FEBS Lett , vol.331 , pp. 134-140
    • Bode, W.1    Gomis-Rüth, F.-X.2    Stöcker, W.3
  • 6
    • 0028324076 scopus 로고
    • The crystal structure of human neutrophil collagenase inhibited by a substrate analog reveals the essentials for catalysis and specificity
    • Bode W, Reinemer P, Huber R, Kleine T, Schnierer S, Tschesche H. 1994. The crystal structure of human neutrophil collagenase inhibited by a substrate analog reveals the essentials for catalysis and specificity. EMBO J 13:1263-1269.
    • (1994) EMBO J , vol.13 , pp. 1263-1269
    • Bode, W.1    Reinemer, P.2    Huber, R.3    Kleine, T.4    Schnierer, S.5    Tschesche, H.6
  • 8
    • 0029030448 scopus 로고
    • Matrilysin-inhibitor complexes: Common themes among metalloproteases
    • Browner MF, Smith WW, Castelhano AL. 1995. Matrilysin-inhibitor complexes: Common themes among metalloproteases. Biochemistry 34:6602-6610.
    • (1995) Biochemistry , vol.34 , pp. 6602-6610
    • Browner, M.F.1    Smith, W.W.2    Castelhano, A.L.3
  • 9
    • 0002208132 scopus 로고
    • Crystallographic refinement by simulated annealing-application to crambin
    • Brünger AT, Karplus M, Petsko GA. 1989. Crystallographic refinement by simulated annealing-application to crambin. Acta Cryst Sect A45:50-61.
    • (1989) Acta Cryst Sect , vol.A45 , pp. 50-61
    • Brünger, A.T.1    Karplus, M.2    Petsko, G.A.3
  • 11
    • 0027251836 scopus 로고
    • A synthetic matrix metalloproteinase inhibitor decreases tumor burden and prolongs survival of mice bearing human ovarian carcinoma xenografts
    • Davies B, Brown PD, East N, Crimmin M, Balkwill FR. 1993. A synthetic matrix metalloproteinase inhibitor decreases tumor burden and prolongs survival of mice bearing human ovarian carcinoma xenografts. Cancer Res 53:2087-2091.
    • (1993) Cancer Res , vol.53 , pp. 2087-2091
    • Davies, B.1    Brown, P.D.2    East, N.3    Crimmin, M.4    Balkwill, F.R.5
  • 13
    • 0027724599 scopus 로고
    • Galardin™
    • Galardy RE. 1993. Galardin™. Drugs Future 18:1109-1111.
    • (1993) Drugs Future , vol.18 , pp. 1109-1111
    • Galardy, R.E.1
  • 14
    • 0028838862 scopus 로고
    • Structural determination and analysis of human neutrophil collagenase complexed with a hydroxamate inhibitor
    • Grams F, Crimmin M, Hinnes L, Huxley P, Pieper M, Tschesche H, Bode W. 1995a. Structural determination and analysis of human neutrophil collagenase complexed with a hydroxamate inhibitor. Biochemistry 34:14012-14020.
    • (1995) Biochemistry , vol.34 , pp. 14012-14020
    • Grams, F.1    Crimmin, M.2    Hinnes, L.3    Huxley, P.4    Pieper, M.5    Tschesche, H.6    Bode, W.7
  • 15
    • 0028915695 scopus 로고
    • X-ray structures of human neutrophil collagenase complexed with peptide hydroxamate and peptide thiol inhibitors - Implications for substrate-binding and rational drug design
    • Grams F, Reinemer P, Powers JC, Kleine T, Tschesche H, Bode W. 1995b. X-ray structures of human neutrophil collagenase complexed with peptide hydroxamate and peptide thiol inhibitors - Implications for substrate-binding and rational drug design. Eur J Biochem 228:830-841.
    • (1995) Eur J Biochem , vol.228 , pp. 830-841
    • Grams, F.1    Reinemer, P.2    Powers, J.C.3    Kleine, T.4    Tschesche, H.5    Bode, W.6
  • 16
    • 0023619941 scopus 로고
    • Collagenase inhibitors: Their design and potential therapeutic use
    • Johnson WH, Roberts NA, Borkakoti N. 1987. Collagenase inhibitors: Their design and potential therapeutic use. J Enzyme Inhibition 2:1-22.
    • (1987) J Enzyme Inhibition , vol.2 , pp. 1-22
    • Johnson, W.H.1    Roberts, N.A.2    Borkakoti, N.3
  • 17
    • 0025190464 scopus 로고
    • Phosphoramidate peptide inhibitors of human skin fibroblast collagenase
    • Kortylewicz ZP, Galardy RE. 1990. Phosphoramidate peptide inhibitors of human skin fibroblast collagenase. J Med Chem 33:263-273.
    • (1990) J Med Chem , vol.33 , pp. 263-273
    • Kortylewicz, Z.P.1    Galardy, R.E.2
  • 20
    • 0027257103 scopus 로고
    • Comparative sequence specificities of human 72- and 92-kDa gelatinases (type IV collagenases) and PUMP (matrilysin)
    • Netzel-Arnett S, Sang Q-X, Moore WGI, Navre M, Birkedal-Hansen H, van Wart HE. 1993. Comparative sequence specificities of human 72-and 92-kDa gelatinases (type IV collagenases) and PUMP (matrilysin). Biochemistry 32:6427-6432.
    • (1993) Biochemistry , vol.32 , pp. 6427-6432
    • Netzel-Arnett, S.1    Sang, Q.-X.2    Moore, W.G.I.3    Navre, M.4    Birkedal-Hansen, H.5    Van Wart, H.E.6
  • 21
    • 0027050785 scopus 로고
    • Substrate specificity of the human matrix metalloproteinase stromelysin and the development of continuous fluorometric assays
    • Niedzwiecki L, Teahan J, Harrison RK, Stein RL. 1992. Substrate specificity of the human matrix metalloproteinase stromelysin and the development of continuous fluorometric assays. Biochemistry 31:12618-12623.
    • (1992) Biochemistry , vol.31 , pp. 12618-12623
    • Niedzwiecki, L.1    Teahan, J.2    Harrison, R.K.3    Stein, R.L.4
  • 25
    • 0028969678 scopus 로고
    • The metzincins - Topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zinc-peptidases
    • Stöcker W, Grams F, Baumann U, Reinemer P, Gomis-Rüth F-X, McKay DB, Bode W. 1995. The metzincins - Topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zinc-peptidases. Protein Sci 4:823-840.
    • (1995) Protein Sci , vol.4 , pp. 823-840
    • Stöcker, W.1    Grams, F.2    Baumann, U.3    Reinemer, P.4    Gomis-Rüth, F.-X.5    McKay, D.B.6    Bode, W.7
  • 26
    • 0031081961 scopus 로고    scopus 로고
    • C-H⋯O hydrogen bonding in biology
    • Wahl MC, Sundaralingam M. 1997. C-H⋯O hydrogen bonding in biology. Trends Biosci 22:97-101.
    • (1997) Trends Biosci , vol.22 , pp. 97-101
    • Wahl, M.C.1    Sundaralingam, M.2
  • 27
    • 0025847582 scopus 로고
    • Matrix metalloproteinases and their inhibitors in connective tissue remodeling
    • Woessner JF Jr. 1991. Matrix metalloproteinases and their inhibitors in connective tissue remodeling. FASEB J 5:2145-2154.
    • (1991) FASEB J , vol.5 , pp. 2145-2154
    • Woessner Jr., J.F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.