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Volumn 362, Issue 1, 2006, Pages 78-88

Crystal Structure of an Active Form of Human MMP-1

Author keywords

collagen; fibroblast collagenase; inhibitor free; matrix metalloproteinases; X ray crystallography

Indexed keywords

HEMOPEXIN; INTERSTITIAL COLLAGENASE; WATER; ZINC;

EID: 33747610734     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.06.079     Document Type: Article
Times cited : (90)

References (31)
  • 1
    • 0033618337 scopus 로고    scopus 로고
    • Matrix metalloproteinases
    • Nagase H., and Woessner J.F. Matrix metalloproteinases. J. Biol. Chem. 274 (1999) 21491-21494
    • (1999) J. Biol. Chem. , vol.274 , pp. 21491-21494
    • Nagase, H.1    Woessner, J.F.2
  • 2
    • 0033848986 scopus 로고    scopus 로고
    • Matrix metalloproteinases: effectors of development and normal physiology
    • Vu T.H., and Werb Z. Matrix metalloproteinases: effectors of development and normal physiology. Genes Dev. 14 (2000) 2123-2133
    • (2000) Genes Dev. , vol.14 , pp. 2123-2133
    • Vu, T.H.1    Werb, Z.2
  • 3
    • 0037693895 scopus 로고    scopus 로고
    • Matrix metalloproteinases and tissue inhibitors of metalloproteinases: structure, function, and biochemistry
    • Visse R., and Nagase H. Matrix metalloproteinases and tissue inhibitors of metalloproteinases: structure, function, and biochemistry. Circulation Res. 92 (2003) 827-839
    • (2003) Circulation Res. , vol.92 , pp. 827-839
    • Visse, R.1    Nagase, H.2
  • 5
    • 0028947020 scopus 로고
    • Matrix metalloproteinase-2 is an interstitial collagenase. Inhibitor-free enzyme catalyzes the cleavage of collagen fibrils and soluble native type I collagen generating the specific 3/4- and 1/4-length fragments
    • Aimes R.T., and Quigley J.P. Matrix metalloproteinase-2 is an interstitial collagenase. Inhibitor-free enzyme catalyzes the cleavage of collagen fibrils and soluble native type I collagen generating the specific 3/4- and 1/4-length fragments. J. Biol. Chem. 270 (1995) 5872-5876
    • (1995) J. Biol. Chem. , vol.270 , pp. 5872-5876
    • Aimes, R.T.1    Quigley, J.P.2
  • 6
    • 0031025218 scopus 로고    scopus 로고
    • Membrane type 1 matrix metalloproteinase digests interstitial collagens and other extracellular matrix molecules
    • Ohuchi E., Imai K., Fujii Y., Sato H., Seiki M., and Okada Y. Membrane type 1 matrix metalloproteinase digests interstitial collagens and other extracellular matrix molecules. J. Biol. Chem. 272 (1997) 2446-2451
    • (1997) J. Biol. Chem. , vol.272 , pp. 2446-2451
    • Ohuchi, E.1    Imai, K.2    Fujii, Y.3    Sato, H.4    Seiki, M.5    Okada, Y.6
  • 7
    • 0029766216 scopus 로고    scopus 로고
    • Metalloproteinase inhibitors and the prevention of connective tissue breakdown
    • Cawston T.E. Metalloproteinase inhibitors and the prevention of connective tissue breakdown. Pharmacol. Ther. 70 (1996) 163-182
    • (1996) Pharmacol. Ther. , vol.70 , pp. 163-182
    • Cawston, T.E.1
  • 8
    • 0032227612 scopus 로고    scopus 로고
    • Role of matrix proteases in processing enamel proteins
    • Woessner J.F. Role of matrix proteases in processing enamel proteins. Connective Tissue Res. 39 (1998) 141-149
    • (1998) Connective Tissue Res. , vol.39 , pp. 141-149
    • Woessner, J.F.1
  • 9
    • 0035188727 scopus 로고    scopus 로고
    • How matrix metalloproteinases regulate cell behaviour
    • Sternlicht M.D., and Werb Z. How matrix metalloproteinases regulate cell behaviour. Annu. Rev. Cell Dev. Biol. 17 (2001) 463-516
    • (2001) Annu. Rev. Cell Dev. Biol. , vol.17 , pp. 463-516
    • Sternlicht, M.D.1    Werb, Z.2
  • 10
    • 0036516460 scopus 로고    scopus 로고
    • Matrix metalloproteinases: a tail of a frog that became a prince
    • Brinckerhoff C.E., and Matrisian L.M. Matrix metalloproteinases: a tail of a frog that became a prince. Nature Rev. Mol. Cell Biol. 3 (2002) 207-214
    • (2002) Nature Rev. Mol. Cell Biol. , vol.3 , pp. 207-214
    • Brinckerhoff, C.E.1    Matrisian, L.M.2
  • 11
    • 0024461448 scopus 로고
    • Fragments of fibroblast collagenase. Purification and characterisation
    • Clark I.M., and Cawston T.E. Fragments of fibroblast collagenase. Purification and characterisation. Biochem. J. 263 (1989) 201-206
    • (1989) Biochem. J. , vol.263 , pp. 201-206
    • Clark, I.M.1    Cawston, T.E.2
  • 12
    • 0029644935 scopus 로고
    • Structure of full-length porcine synovial collagenase reveals a C-terminal domain containing a calcium-linked, four bladed β-propeller
    • Li J., Brick P., O'Hare M.C., Skarzynski T., Lloyd L.F., Curry V.A., et al. Structure of full-length porcine synovial collagenase reveals a C-terminal domain containing a calcium-linked, four bladed β-propeller. Structure 3 (1995) 541-549
    • (1995) Structure , vol.3 , pp. 541-549
    • Li, J.1    Brick, P.2    O'Hare, M.C.3    Skarzynski, T.4    Lloyd, L.F.5    Curry, V.A.6
  • 15
    • 0025026410 scopus 로고
    • Mechanisms of activation of tissue procollagenase by matrix metalloproteinase 3 (stromelysin)
    • Suzuki K., Enghild J.J., Morodomi T., Salvesen G., and Nagase H. Mechanisms of activation of tissue procollagenase by matrix metalloproteinase 3 (stromelysin). Biochemistry 29 (1990) 10261-10270
    • (1990) Biochemistry , vol.29 , pp. 10261-10270
    • Suzuki, K.1    Enghild, J.J.2    Morodomi, T.3    Salvesen, G.4    Nagase, H.5
  • 16
    • 0028040070 scopus 로고
    • Structural implications for the role of the N terminus in the 'superactivation' of collagenases. A crystallographic study
    • Reinemer P., Grams F., Huber R., Kleine T., Schnierer S., Pipes M., et al. Structural implications for the role of the N terminus in the 'superactivation' of collagenases. A crystallographic study. FEBS Letters 338 (1994) 227-233
    • (1994) FEBS Letters , vol.338 , pp. 227-233
    • Reinemer, P.1    Grams, F.2    Huber, R.3    Kleine, T.4    Schnierer, S.5    Pipes, M.6
  • 17
    • 0030957218 scopus 로고    scopus 로고
    • Activation mechanisms of matrix metalloproteinases
    • Nagase H. Activation mechanisms of matrix metalloproteinases. Biol. Chem. 378 (1997) 151-160
    • (1997) Biol. Chem. , vol.378 , pp. 151-160
    • Nagase, H.1
  • 18
    • 0028805811 scopus 로고
    • Stromelysin-1: three dimensional structure of the inhibited catalytic domain and of the C-truncated proenzyme
    • Becker J.W., Marcy A.I., Rokosz L.L., Axel M.G., Burbaum J.J., Fitzgerald P.M.D., et al. Stromelysin-1: three dimensional structure of the inhibited catalytic domain and of the C-truncated proenzyme. Protein Sci. 4 (1995) 1966-1976
    • (1995) Protein Sci. , vol.4 , pp. 1966-1976
    • Becker, J.W.1    Marcy, A.I.2    Rokosz, L.L.3    Axel, M.G.4    Burbaum, J.J.5    Fitzgerald, P.M.D.6
  • 19
    • 0030945404 scopus 로고    scopus 로고
    • Analysis of the contribution of the hinge region of human neutrophil collagenase (HNC, MMP-8) to stability and collagenolytic activity by alanine scanning mutagenesis
    • Knäuper V., Docherty A.J., Smith B., Tschesche H., and Murphy G. Analysis of the contribution of the hinge region of human neutrophil collagenase (HNC, MMP-8) to stability and collagenolytic activity by alanine scanning mutagenesis. FEBS Letters 405 (1997) 60-64
    • (1997) FEBS Letters , vol.405 , pp. 60-64
    • Knäuper, V.1    Docherty, A.J.2    Smith, B.3    Tschesche, H.4    Murphy, G.5
  • 20
    • 0028128235 scopus 로고
    • Crystal structures of recombinant 19-kDa human fibroblast collagenase complexed to itself
    • Lovejoy B., Hassell A.M., Luther M.A., Weigl D., and Jordan S.R. Crystal structures of recombinant 19-kDa human fibroblast collagenase complexed to itself. Biochemistry 33 (1994) 8207-8217
    • (1994) Biochemistry , vol.33 , pp. 8207-8217
    • Lovejoy, B.1    Hassell, A.M.2    Luther, M.A.3    Weigl, D.4    Jordan, S.R.5
  • 21
    • 0037178891 scopus 로고    scopus 로고
    • Unexpected crucial role of residue 272 in substrate specificity of fibroblast collagenase
    • Tsukada H., and Pourmotabbed T. Unexpected crucial role of residue 272 in substrate specificity of fibroblast collagenase. J. Biol. Chem. 277 (2002) 27378-27384
    • (2002) J. Biol. Chem. , vol.277 , pp. 27378-27384
    • Tsukada, H.1    Pourmotabbed, T.2
  • 23
    • 0034703074 scopus 로고    scopus 로고
    • Identification of the (183)RWTNNFREY(191) region as a critical segment of matrix metalloproteinase 1 for the expression of collagenolytic activity
    • Chung L., Shimokawa K., Dinakarpandian D., Grams F., Fields G.B., and Nagase H. Identification of the (183)RWTNNFREY(191) region as a critical segment of matrix metalloproteinase 1 for the expression of collagenolytic activity. J. Biol. Chem. 275 (2000) 29610-29617
    • (2000) J. Biol. Chem. , vol.275 , pp. 29610-29617
    • Chung, L.1    Shimokawa, K.2    Dinakarpandian, D.3    Grams, F.4    Fields, G.B.5    Nagase, H.6
  • 24
    • 0032913989 scopus 로고    scopus 로고
    • Sequence dependent conformational variations of collagen triple helical structure
    • Kramer R.Z., Bella J., Mayville P., Brodsky B., and Berman H.M. Sequence dependent conformational variations of collagen triple helical structure. Nature Struct. Biol. 6 (1999) 454-457
    • (1999) Nature Struct. Biol. , vol.6 , pp. 454-457
    • Kramer, R.Z.1    Bella, J.2    Mayville, P.3    Brodsky, B.4    Berman, H.M.5
  • 25
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-325
    • (1997) Methods Enzymol. , vol.276 , pp. 307-325
    • Otwinowski, Z.1    Minor, W.2
  • 26
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Collaborative Computational Project
    • Collaborative Computational Project. The CCP4 suite: programs for protein crystallography. Acta Crystallog. sect. D 50 (1994) 760-763
    • (1994) Acta Crystallog. sect. D , vol.50 , pp. 760-763
  • 27
    • 0030864522 scopus 로고    scopus 로고
    • Crystallographic refinement by simulated annealing: methods and applications
    • Brünger A.T., and Rice L.M. Crystallographic refinement by simulated annealing: methods and applications. Methods Enzymol. 277 (1998) 243-268
    • (1998) Methods Enzymol. , vol.277 , pp. 243-268
    • Brünger, A.T.1    Rice, L.M.2
  • 28
    • 0030767713 scopus 로고    scopus 로고
    • Free R value: cross validation in crystallography
    • Brünger A.T. Free R value: cross validation in crystallography. Methods Enzymol. 277 (1997) 366-395
    • (1997) Methods Enzymol. , vol.277 , pp. 366-395
    • Brünger, A.T.1
  • 29
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model building tools for molecular graphics
    • Emsley P., and Cowtan K. Coot: model building tools for molecular graphics. Acta Crystallog. sect. D 60 (2004) 2126-2132
    • (2004) Acta Crystallog. sect. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 30
    • 0026244229 scopus 로고
    • MOLSCRIPT-a program to produce both detailed and schematic plots of protein structures
    • Kraulis P.J. 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
  • 31
    • 0028304962 scopus 로고
    • Satisfying hydrogen bonding potential in proteins
    • McDonald I.K., and Thornton J.M. Satisfying hydrogen bonding potential in proteins. J. Mol. Biol. 238 (1994) 777-793
    • (1994) J. Mol. Biol. , vol.238 , pp. 777-793
    • McDonald, I.K.1    Thornton, J.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.