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Crystal structure of the complex formed by the membrane type 1-matrix metalloproteinase with the tissue inhibitor of metalloproteinases-2, the soluble progelatinase a receptor.

Fernandez‐Catalan, Carlos, Bode, Wolfram, Huber, Robert, Turk, Dusan, Calvete, Juan J., Lichte, Andrea, Tschesche, Harald, Maskos, Klaus·1998·The EMBO Journal
DOI 10.1093/emboj/17.17.5238
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  • The MT-loop is flexible and only present in the four membrane type MMPs, but the conformation of the MT-loop is different in each membrane type MMP and in MT1-MMP complexed with or without TIMPs.

    “The MT-loop is flexible and only present in the four membrane type MMPs, but the conformation of the MT-loop is different in each membrane type MMP (61) and in MT1-MMP complexed with or without TIMPs (62–64).”

    From Identification of amino acid residues in the MT-loop of MT1-MMP critical for its ability to cleave low-density lipoprotein receptor (2022) · cites this paper as [64]

    The MT1-MMP catalytic domain section (p. 5240) describes the MT-loop as characteristic of MT-MMPs and flexible, and the paper reports its structure in a TIMP-2 complex. It does not establish that the loop adopts a different conformation with and without TIMPs; the Discussion says structural comparisons with the free components must await their structures. (LLM, conf=0.86)

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Research works printed but not linked: 56

  1. Apte SS, Olsen BR and Murphy G (1995) The gene structure of tissue inhibitor of metalloproteinases (TIMP)‐3 and its inhibitory activities define the distinct TIMP gene family. J Biol Chem, 270, 14313–14318. · DOI
  2. Barton GJ (1993) ALSCRIPT: a tool to format multiple sequence alignments. Protein Eng, 6, 37–40. · DOI
  3. Bigg HF, Shi YE, Liu YE, Steffensen B and Overall CM (1997) Specific, high affinity binding of tissue inhibitor of metalloproteinases‐4 (TIMP‐4) to the COOH‐terminal hemopexin‐like domain of human gelatinase A. J Biol Chem, 272, 15496–15500. · DOI
  4. Bode W, Reinemer P, Huber R, Kleine T, Schnierer S and Tschesche H (1994) The X‐ray crystal structure of the catalytic domain of human neutrophil collagenase inhibited by a substrate analogue reveals the essentials for catalysis and specificity. EMBO J, 13, 1263–1269. · DOI
  5. Boone TC, Johnson MJ, De Cle YA and Langley KE (1990) cDNA cloning and expression of a metalloproteinase inhibitor related to tissue inhibitor of metalloproteinases. Proc Natl Acad Sci USA, 87, 2800–2804. · DOI
  6. Brooks PC, Strömblad S, Sanders LC, vonSchalscha TL, Aimes RT, Stetler‐Stevenson WG, Quigley JP and Cheresh DA (1996) Localization of matrix metalloproteinase MMP‐2 to the surface of invasive cells by interaction with integrin αvβ3. Cell, 85, 683–693. · DOI
  7. Brünger AT (1991) Simulated annealing in crystallography. Annu Rev Phys Chem, 42, 197–223. · DOI
  8. Brünger AT (1992) X‐PLOR Version 3.1 A System for X‐Ray Crystallography and NMR. Yale University Press, New Haven, CT.
  9. Butler GS, Will H, Atkinson SJ and Murphy G (1997) Membrane‐type‐2 matrix metalloproteinase can initiate the processing of progelatinase A and is regulated by the tissue inhibitors of metalloproteinases. Eur J Biochem, 244, 653–657. · DOI
  10. Butler GS, Butler MJ, Atkinson SJ, Will H, Tamura T, van Westrum SS, Crabbe T, Clements J, d'Ortho MP and Murphy G (1998) The TIMP2 membrane type 1 metalloproteinase ‘receptor’ regulates the concentration and efficient activation of progelatinase A. J Biol Chem, 273, 871–880. · DOI · Paper page
  11. Calvete JJ, Varela PF, Sanz L, Romero A, Mann K and Töpfer‐Petersen E (1996) A procedure for the large‐scale isolation of major bovine seminal plasma proteins. Protein Expr Purif, 8, 48–56. · DOI
  12. Cao J, Sato H, Takino T and Seiki M (1995) The C‐terminal region of membrane type matrix metalloproteinase is a functional transmembrane domain required for progelatinase A activation. J Biol Chem, 270, 801–805. · DOI
  13. Cawston T (1998) Matrix metalloproteinases and TIMPs: properties and implications for the rheumatic diseases. Mol Med Today, 4, 130–137. · DOI
  14. Collaborative Computational Project Number 4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr D, 50, 760–763. · DOI
  15. Docherty AJP, Lyons A, Smith BJ, Wright EM, Stephens PE, Harris TJR, Murphy G and Reynolds JJ (1985) Sequence of human tissue inhibitor of metalloproteinases and its identity to erythroid potentiating activity. Nature, 318, 65–69.
  16. Engh RA and Huber R (1991) Accurate bond and angle parameters for X‐ray protein structure refinement. Acta Crystallogr A, 47, 392–400. · DOI
  17. Evans SV (1993) SETOR: hardware lighted three‐dimensional solid model representations of macromolecules. J Mol Graph, 11, 134–138. · DOI
  18. Fridman R, Fuerst TR, Bird RE, Hoyhtya M, Oelkuct M, Kraus S, Komarek D, Liotta LA, Berman ML and Stetler‐Stevenson WG (1992) Domain structure of human 72‐kDa gelatinase/typeIV collagenase. J Biol Chem, 267, 15398–15405. · DOI
  19. Gohlke U, Gomis‐Rüth F‐X, Crabbe T, Murphy G, Docherty AJP and Bode W (1996) The C‐terminal (haemopexin‐like) domain structure of human gelatinase A (MMP2): structural implications for its function. FEBS Lett, 378, 126–130. · DOI
  20. Gomez DE, Alonso DF, Yoshiji H and Thorgeirsson UP (1997) Tissue inhibitors of metalloproteinases: structure, regulation and biological functions. Eur J Cell Biol, 74, 111–122.
  21. Gomis‐Rüth FX et al. (1997) Mechanism of inhibition of the human matrix metalloproteinase stromelysin‐1 by TIMP‐1. Nature, 389, 77–81. · DOI · Paper page
  22. Green J, Wang M, Liu YE, Raymond LA, Rosen C and Shi YE (1996) Molecular cloning and characterisation of human tissue inhibitor of metalloproteinase 4. J Biol Chem, 271, 30375–30380. · DOI
  23. Huang W, Meng Q, Suzuki K, Nagase H and Brew K (1997) Mutational study of the amino‐terminal domain of human tissue inhibitor of metalloproteinases 1 (TIMP‐1) locates an inhibitory region for matrix metalloproteinases. J Biol Chem, 272, 22086–22091. · DOI
  24. Kinoshita T, Sato H, Takino T, Itoh M, Akizawa T and Seiki M (1996) Processing of a precursor of 72‐kilodalton type IV collagenase/gelatinase A by a recombinant membrane‐type 1 matrix metalloproteinase. Cancer Res, 56, 2535–2538.
  25. Kolkenbrock H, Orgel D, Hecker‐Kia A, Noack W and Ulbrich N (1991) The complex between a tissue inhibitor of metalloproteinases (TIMP‐2) and 72‐kDa progelatinase is a metalloproteinase inhibitor. Eur J Biochem, 198, 775–781. · DOI
  26. Kolkenbrock H, Hecker‐Kia A, Orgel D, Ruppitsch W and Ulbrich N (1994) Activity of ternary gelatinase A‐TIMP‐2‐matrix metalloproteinase complexes. Biol Chem Hoppe‐Seyler, 375, 241–247. · DOI
  27. Kraulis PJ (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of proteins. J Appl Crystallogr, 24, 946–950. · DOI
  28. Li J‐Y et al. (1995) Structure of full‐length porcine synovial collagenase reveals a C‐terminal domain containing a calcium‐linked, four‐bladed beta‐propeller. Structure, 3, 541–549. · DOI
  29. Lichte A, Kolkenbrock H and Tschesche H (1996) The recombinant catalytic domain of membrane‐type matrix metalloproteinase‐1 (MT1‐MMP) induces activation of progelatinase A and progelatinase A complexed with TIMP‐2. FEBS Lett, 397, 277–282. · DOI
  30. Mucha A, Cunisse P, Kannan R, Beau F, Yiotakis A, Basset P and Dive V (1998) Membrane type‐1 matrix metalloprotease and stromelysin‐3 cleave more efficiently synthetic substrates containing unusual amino acids in their P1′ positions. J Biol Chem, 273, 2763–2768. · DOI
  31. Murphy G and Willenbrock F (1995) Tissue inhibitors of matrix metalloendopeptidases. Methods Enzymol, 248, 496–510. · DOI
  32. Murphy G, Willenbrock F, Ward RV, Cockett MI, Eaton D and Docherty AJP (1992) The C‐terminal domain of 72 kDa gelatinase A is not required for catalysis, but is essential for membrane activation and modulates interactions with tissue inhibitors of metalloproteinases. Biochem J, 283, 637–641. · DOI
  33. Nagase H (1997) Activation mechanisms of matrix metalloproteinases. Biol Chem, 378, 151–160.
  34. Navaza J (1994) AMoRe: an automated package for molecular replacement. Acta Crystallogr Sect A 50, 157–163. · DOI
  35. Nicholls A, Bharadwaj R and Honig B (1993) Grasp—graphical representation and analysis of surface properties. Biophys J, 64, A166.
  36. Ohuchi E, Imai K, Fujii Y, Sato H, Seiki M and Okada Y (1997) Membrane type 1 matrix metalloproteinase digests interstitial collagens and other extracellular matrix macromolecules. J Biol Chem, 272, 2446–2451. · DOI · Paper page
  37. Okada A, Bellocq J‐P, Rouyer N, Chenard M‐P, Rio M‐C, Chambon P and Basset P (1995) Membrane‐type matrix metalloproteinase (MT‐MMP) gene is expressed in stromal cells of human colon, breast and head and neck carcinomas. Proc Natl Acad Sci USA, 92, 2730–2734. · DOI
  38. Olson MW, Gervasi DC, Mobasheri S and Fridman R (1997) Kinetic analysis of the binding of human matrix metalloproteinase‐2 and ‐9 to tissue inhibitor of metalloproteinase (TIMP)‐1 and TIMP‐2. J Biol Chem, 272, 29975–29983. · DOI
  39. d'Ortho M‐P, Will H, Atkinson S, Butler G, Messent A, Gavrilovic J, Smith B, Timpl R, Zardi L and Murphy G (1997) Membrane‐type matrix metalloproteinases 1 and 2 exhibit broad‐spectrum proteolytic capacities comparable to many matrix metalloproteinases. Eur J Biochem, 250, 751–757. · DOI
  40. Otwinowski Z and Minor W (1993) DENZO: A Film Processing for Macromolecular Crystallography. Yale University, New Haven, CT.
  41. Pei D and Weiss SJ (1996) Transmembrane‐deletion mutants of the membrane‐type matrix metalloproteinase‐1 process progelatinase A and express intrinsic matrix‐degrading activity. J Biol Chem, 271, 9135–9140. · DOI
  42. Reinemer P, Grams F, Huber R, Kleine T, Schnierer S, Pieper M, Tschesche H and Bode W (1994) Structural implications for the role of the N‐terminus in the ‘superactivation’ of collagenases—a crystallographic study. FEBS Lett, 338, 227–233. · DOI
  43. Sato H, Takino T, Okada Y, Cao J, Shinagawa A, Yamamoto E and Seiki M (1994) A matrix metalloproteinase expressed on the surface of invasive tumour cells. Nature, 370, 61–65. · DOI
  44. Sato H, Kinoshita T, Takino T, Nakayama K and Seiki M (1996) Activation of a recombinant membrane type 1‐matrix metalloproteinase (MT1‐MMP) by furin and its interaction with tissue inhibitor of metalloproteinases (TIMP)‐2. FEBS Lett, 393, 101–104. · DOI
  45. Stetler‐Stevenson WG, Krutzsch HC and Liotta LA (1989) Tissue inhibitor of metalloproteinase (TIMP‐2). J Biol Chem, 264, 17374–17378. · DOI
  46. Strongin AY, Marmer BL, Grant GA and Goldberg GI (1993) Plasma membrane‐dependent activation of the 72‐kDa type IV collagenase is prevented by complex formation with TIMP‐2. J Biol Chem, 268, 14033–14039. · DOI
  47. Strongin AY, Collier IE, Bannikov U, Marmer BL, Grant GA and Goldberg GI (1995) Mechanism of cell surface activation of 72‐kDa type IV collagenase. J Biol Chem, 270, 5331–5338. · DOI
  48. Takino T, Sato H, Shinagawa A and Seiki M (1995) Identification of the second membrane‐type matrix metalloproteinase (MT‐MMP‐2) gene from a human placenta cDNA library. J Biol Chem, 270, 23013–23020. · DOI
  49. Turk D (1992) Dissertation, TU München.
  50. Will H and Hinzmann B (1995) cDNA sequence and mRNA tissue distribution of a novel human MMP with a transmembrane segment. Eur J Biochem, 231, 602–608. · DOI
  51. Will H, Atkinson SJ, Butler GS, Smyth B and Murphy G (1996) The soluble catalytic domain of membrane type 1 matrix metalloproteinase cleaves the propeptide of progelatinase A and initiates autocatalytic activation. J Biol Chem, 271, 17119–17123. · DOI
  52. Willenbrock F, Crabbe T, Slowcombe MP, Sutton CW, Docherty AJP, Cockett MI, O'Shea M, Brocklehurst K, Phillips IR and Murphy G (1993) The activity of the tissue inhibitors of metalloproteinases is regulated by C‐terminal domain interactions: a kinetic analysis of the inhibition of gelatinase A. Biochemistry, 32, 4330–4337. · DOI
  53. Williamson RA, Martorell G, Carr MD, Murphy G, Docherty AJ, Freedman RB and Feeney J (1994) Solution structure of the active domain of tissue inhibitor of metalloproteinases‐2. A new member of the OB fold protein family. Biochemistry, 33, 11745–11759. · DOI
  54. Williamson RA, Carr MD, Frenkiel TA, Feeney J and Freedman RB (1997) Mapping the binding site for matrix metalloproteinase on the N‐terminal domain of the tissue inhibitor of metalloproteinases‐2 by NMR chemical shift perturbation. Biochemistry, 36, 13882–13889. · DOI
  55. Woessner JF,Jr (1991) Matrix metalloproteinases and their inhibitors in connective tissue remodeling. FASEB J, 5, 2145–2155. · DOI
  56. Zucker S, Drews M, Conner C, Foda HD, DeClerck YA, Langley KE, Bahou WF, Docherty AJP and Cao J (1998) Tissue inhibitor of metalloproteinase‐2 (TIMP‐2) binds to the catalytic domain of the cell surface receptor, membrane type 1‐matrix metalloproteinase 1 (MT1‐MMP). J Biol Chem, 273, 1216–1222. · DOI

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Metadata

Authors
Fernandez‐Catalan, C., Bode, W., Huber, R., Turk, D., Calvete, J. J., Lichte, A., Tschesche, H., & Maskos, K.
Venue
The EMBO Journal
Publisher
Springer Science and Business Media LLC
Published
1998-09-01
Volume
17
Issue
17
Pages
5238-5248
ISSN
  • 0261-4189
  • 1460-2075
DOI
10.1093/emboj/17.17.5238
Cited by
321
References
1
Language
en
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