메뉴 건너뛰기




Volumn 43, Issue 27, 2004, Pages 8636-8643

Structure of the plasminogen kringle 4 binding calcium-free form of the C-type lectin-like domain of tetranectin

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; CONFORMATIONS; NUCLEAR MAGNETIC RESONANCE; PROTEINS;

EID: 3042854201     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi049570s     Document Type: Article
Times cited : (21)

References (40)
  • 1
    • 0022534552 scopus 로고
    • Purification and characterization of a novel, oligomeric, plasminogen kringle 4 binding protein from human plasma: Tetranectin
    • Clemmensen, I., Petersen, L. C., and Kluft, C. (1986) Purification and characterization of a novel, oligomeric, plasminogen kringle 4 binding protein from human plasma: Tetranectin, Eur. J. Biochem. 156, 327-333.
    • (1986) Eur. J. Biochem. , vol.156 , pp. 327-333
    • Clemmensen, I.1    Petersen, L.C.2    Kluft, C.3
  • 2
    • 0023607273 scopus 로고
    • Plasma tetranectin in healthy male and female individuals, measured by enzyme-linked immunosorbent assay
    • Jensen, B. A., McNair, P., Hyldstrup, L., and Clemmensen, I. (1987) Plasma tetranectin in healthy male and female individuals, measured by enzyme-linked immunosorbent assay, J. Lab. Clin. Med. 110, 612-617.
    • (1987) J. Lab. Clin. Med. , vol.110 , pp. 612-617
    • Jensen, B.A.1    McNair, P.2    Hyldstrup, L.3    Clemmensen, I.4
  • 3
    • 0032239442 scopus 로고    scopus 로고
    • Human tetranectin: Methodological and clinical studies
    • Høgdall, C. K. (1998) Human tetranectin: Methodological and clinical studies, APMIS Suppl. 86, 1-31.
    • (1998) APMIS Suppl. , vol.86 , pp. 1-31
    • Høgdall, C.K.1
  • 4
    • 0028775795 scopus 로고
    • Tetranectin, a plasma and tissue protein-a prognostic marker of breast and ovarian cancer
    • Høgdall, C. K., Christensen, L., and Clemmensen, I. (1994) Tetranectin, a plasma and tissue protein-a prognostic marker of breast and ovarian cancer, Ugeskr. Laeg. 156, 6190-6195.
    • (1994) Ugeskr. Laeg. , vol.156 , pp. 6190-6195
    • Høgdall, C.K.1    Christensen, L.2    Clemmensen, I.3
  • 5
    • 0026731099 scopus 로고
    • Tetranectin, a plasminogen kringle 4-binding protein. Cloning and gene expression pattern in human colon cancer
    • Wewer, U. M., and Albrechtsen, R. (1992) Tetranectin, a plasminogen kringle 4-binding protein. Cloning and gene expression pattern in human colon cancer, Lab. Invest. 67, 253-262.
    • (1992) Lab. Invest. , vol.67 , pp. 253-262
    • Wewer, U.M.1    Albrechtsen, R.2
  • 7
    • 0032529362 scopus 로고    scopus 로고
    • Tetranectin is a novel marker for myogenesis during embryonic development, muscle regeneration, and muscle cell differentiation in vitro
    • Wewer, U. M., Iba, K., Durkin, M. E., Nielsen, F. C., Loechel, F., Gilpin, B. J., Kuang, W., Engvall, E., and Albrechtsen, R. (1998) Tetranectin is a novel marker for myogenesis during embryonic development, muscle regeneration, and muscle cell differentiation in vitro, Dev. Biol. 200, 247-259.
    • (1998) Dev. Biol. , vol.200 , pp. 247-259
    • Wewer, U.M.1    Iba, K.2    Durkin, M.E.3    Nielsen, F.C.4    Loechel, F.5    Gilpin, B.J.6    Kuang, W.7    Engvall, E.8    Albrechtsen, R.9
  • 8
    • 0028980666 scopus 로고
    • Transforming growth factor-b1 downregulates dexamethasone-induced tetranectin gene expression during the in vitro mineralization of the human osteoblastic cell line SV-HFO
    • Iba, K., Sawada, N., Chiba, H., Wewer, U. M., Ishii, S., and Mofi, M. (1995) Transforming growth factor-b1 downregulates dexamethasone-induced tetranectin gene expression during the in vitro mineralization of the human osteoblastic cell line SV-HFO, FEBS Lett. 373, 1-4.
    • (1995) FEBS Lett. , vol.373 , pp. 1-4
    • Iba, K.1    Sawada, N.2    Chiba, H.3    Wewer, U.M.4    Ishii, S.5    Mofi, M.6
  • 12
    • 0034176370 scopus 로고    scopus 로고
    • The heparin-binding site in tetranectin is located in the N-terminal region and binding does not involve the carbohydrate recognition domain
    • Lorentsen, R. H., Graversen, J. H., Caterer, N. R., Thøgersen, H. C., and Etzerodt, M. (2000) The heparin-binding site in tetranectin is located in the N-terminal region and binding does not involve the carbohydrate recognition domain, Biochem. J. 347 (Part 1), 83-87.
    • (2000) Biochem. J. , vol.347 , Issue.PART 1 , pp. 83-87
    • Lorentsen, R.H.1    Graversen, J.H.2    Caterer, N.R.3    Thøgersen, H.C.4    Etzerodt, M.5
  • 15
    • 0032582499 scopus 로고    scopus 로고
    • The plasminogen binding site of the C-type lectin tetranectin is located in the carbohydrate recognition domain, and binding is sensitive to both calcium and lysine
    • Graversen, J. H., Lorentsen, R. H., Jacobsen, C., Moestrup, S. K., Sigurskjold, B. W., Thøgersen, H. C., and Etzerodt, M. (1998) The plasminogen binding site of the C-type lectin tetranectin is located in the carbohydrate recognition domain, and binding is sensitive to both calcium and lysine, J. Biol. Chem. 273, 29241-29246.
    • (1998) J. Biol. Chem. , vol.273 , pp. 29241-29246
    • Graversen, J.H.1    Lorentsen, R.H.2    Jacobsen, C.3    Moestrup, S.K.4    Sigurskjold, B.W.5    Thøgersen, H.C.6    Etzerodt, M.7
  • 16
    • 0034720735 scopus 로고    scopus 로고
    • Tetranectin-binding site on plasminogen kringle 4 involves the lysine-binding pocket and at least one additional amino acid residue
    • Graversen, J. H., Sigurskjold, B. W., Thøgersen, H. C., and Etzerodt, M. (2000) Tetranectin-binding site on plasminogen kringle 4 involves the lysine-binding pocket and at least one additional amino acid residue, Biochemistry 39, 7414-7419.
    • (2000) Biochemistry , vol.39 , pp. 7414-7419
    • Graversen, J.H.1    Sigurskjold, B.W.2    Thøgersen, H.C.3    Etzerodt, M.4
  • 17
    • 0024309645 scopus 로고
    • Functional analogy between lipoprotein(a) and plasminogen in the binding to the kringle 4 binding protein, tetranectin
    • Kluft, C., Jie, A. F., Los, P., de Wit, E., and Havekes, L. (1989) Functional analogy between lipoprotein(a) and plasminogen in the binding to the kringle 4 binding protein, tetranectin, Biochem. Biophys. Res. Commun. 161, 427-433.
    • (1989) Biochem. Biophys. Res. Commun. , vol.161 , pp. 427-433
    • Kluft, C.1    Jie, A.F.2    Los, P.3    De Wit, E.4    Havekes, L.5
  • 20
  • 22
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: A multidimensional spectral processing system based on UNIX pipes, J. Biomol. NMR 6, 277-293.
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 23
    • 0028673711 scopus 로고
    • Automated and semiautomated analysis of homo- and heteronuclear multidimensional nuclear magnetic resonance spectra of proteins: The program Pronto
    • Kjær, M., Andersen, K. V., and Poulsen, F. M. (1994) Automated and semiautomated analysis of homo- and heteronuclear multidimensional nuclear magnetic resonance spectra of proteins: The program Pronto, Methods Enzymol. 239, 288-307.
    • (1994) Methods Enzymol. , vol.239 , pp. 288-307
    • Kjær, M.1    Andersen, K.V.2    Poulsen, F.M.3
  • 25
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi, R., Billeter, M., and Wüthrich, K. (1996) MOLMOL: A program for display and analysis of macromolecular structures, J. Mol. Graphics 14, 51-55 and 29-32.
    • (1996) J. Mol. Graphics , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 27
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • Güntert, P., Mumenthaler, C., and Wüthrich, K. (1997) Torsion angle dynamics for NMR structure calculation with the new program DYANA, J. Mol. Biol. 273, 283-298.
    • (1997) J. Mol. Biol. , vol.273 , pp. 283-298
    • Güntert, P.1    Mumenthaler, C.2    Wüthrich, K.3
  • 28
    • 0036308102 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA
    • Herrmann, T., Güntert, P., and Wüthrich, K. (2002) Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA, J. Mol. Biol. 319, 209-227.
    • (2002) J. Mol. Biol. , vol.319 , pp. 209-227
    • Herrmann, T.1    Güntert, P.2    Wüthrich, K.3
  • 29
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • Cornilescu, G., Delaglio, F., and Bax, A. (1999) Protein backbone angle restraints from searching a database for chemical shift and sequence homology, J. Biomol. NMR 13, 289-302.
    • (1999) J. Biomol. NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 33
    • 0032558935 scopus 로고    scopus 로고
    • 2+-dependent structural changes in C-type mannose-binding proteins
    • 2+- dependent structural changes in C-type mannose-binding proteins, Biochemistry 37, 17965-17976.
    • (1998) Biochemistry , vol.37 , pp. 17965-17976
    • Ng, K.K.1    Park-Snyder, S.2    Weis, W.I.3
  • 34
    • 0034647695 scopus 로고    scopus 로고
    • Structure of a C-type carbohydrate recognition domain from the macrophage mannose receptor
    • Feinberg, H., Park-Snyder, S., Kolatkar, A. R., Heise, C. T., Taylor, M. E., and Weis, W. I. (2000) Structure of a C-type carbohydrate recognition domain from the macrophage mannose receptor, J. Biol. Chem. 275, 21539-21548.
    • (2000) J. Biol. Chem. , vol.275 , pp. 21539-21548
    • Feinberg, H.1    Park-Snyder, S.2    Kolatkar, A.R.3    Heise, C.T.4    Taylor, M.E.5    Weis, W.I.6
  • 35
    • 0028113016 scopus 로고
    • Characterization of ligand binding to a carbohydrate-recognition domain of the macrophage mannose receptor
    • Mullin, N. P., Hall, K. T., and Taylor, M. E. (1994) Characterization of ligand binding to a carbohydrate-recognition domain of the macrophage mannose receptor, J. Biol. Chem. 269, 28405-28413.
    • (1994) J. Biol. Chem. , vol.269 , pp. 28405-28413
    • Mullin, N.P.1    Hall, K.T.2    Taylor, M.E.3
  • 36
    • 0032558977 scopus 로고    scopus 로고
    • Coupling of prolyl peptide bond isomerization and Ca2+ binding in a C-type mannose-binding protein
    • Ng, K. K., and Weis, W. I. (1998) Coupling of prolyl peptide bond isomerization and Ca2+ binding in a C-type mannose-binding protein, Biochemistry 37, 17977-17989.
    • (1998) Biochemistry , vol.37 , pp. 17977-17989
    • Ng, K.K.1    Weis, W.I.2
  • 37
    • 0035909099 scopus 로고    scopus 로고
    • The ligand-binding loops in the tunicate C-type lectin TC14 are rigid
    • Poget, S. F., Freund, S. M. V., Howard, M. J., and Bycroft, M. (2001) The ligand-binding loops in the tunicate C-type lectin TC14 are rigid, Biochemistry 40, 10966-10972.
    • (2001) Biochemistry , vol.40 , pp. 10966-10972
    • Poget, S.F.1    Freund, S.M.V.2    Howard, M.J.3    Bycroft, M.4
  • 38
    • 0032775212 scopus 로고    scopus 로고
    • The structure of a tunicate C-type lectin from Polyandrocarpa misakiensis complexed with D-galactose
    • Poget, S. F., Legge, G. B., Proctor, M. R., Butler, P. J., Bycroft, M., and Williams, R. L. (1999) The structure of a tunicate C-type lectin from Polyandrocarpa misakiensis complexed with D-galactose, J. Mol. Biol. 290, 867-879.
    • (1999) J. Mol. Biol. , vol.290 , pp. 867-879
    • Poget, S.F.1    Legge, G.B.2    Proctor, M.R.3    Butler, P.J.4    Bycroft, M.5    Williams, R.L.6
  • 39
    • 0035138842 scopus 로고    scopus 로고
    • Extracellular calcium sensing and extracellular calcium signaling
    • Brown, E. M., and MacLeod, R. J. (2001) Extracellular calcium sensing and extracellular calcium signaling, Physiol. Rev. 81, 239-297.
    • (2001) Physiol. Rev. , vol.81 , pp. 239-297
    • Brown, E.M.1    MacLeod, R.J.2
  • 40
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex, N., and Peitsch, M. C. (1997) SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling, Electrophoresis 18, 2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.