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Volumn 302, Issue 4, 2003, Pages 849-854

The structure and function of human dipeptidyl peptidase IV, possessing a unique eight-bladed β-propeller fold

Author keywords

Dipeptidyl peptidase IV; Prolyl oligopeptidase; Serine protease; X ray crystal structure; Propeller fold

Indexed keywords

DIPEPTIDYL PEPTIDASE IV; PROLYL ENDOPEPTIDASE;

EID: 0037459171     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-291X(03)00258-4     Document Type: Article
Times cited : (94)

References (26)
  • 1
    • 0021273620 scopus 로고
    • Evolution of proteolytic enzymes
    • Neurath H. Evolution of proteolytic enzymes. Science. 224:1984;350-357.
    • (1984) Science , vol.224 , pp. 350-357
    • Neurath, H.1
  • 2
    • 0018801053 scopus 로고
    • Susceptibility of a peptide derived from bradykinin to hydrolysis by brain endo-oligopeptidases and pancreatic proteinases
    • Camargo A.C., Caldo H., Reis M.L. Susceptibility of a peptide derived from bradykinin to hydrolysis by brain endo-oligopeptidases and pancreatic proteinases. J. Biol. Chem. 254:1979;5304-5307.
    • (1979) J. Biol. Chem. , vol.254 , pp. 5304-5307
    • Camargo, A.C.1    Caldo, H.2    Reis, M.L.3
  • 3
    • 0016770479 scopus 로고
    • Protease II from Escherichia coli. Purification and characterization
    • Pacaud M., Richaud C. Protease II from Escherichia coli. Purification and characterization. J. Biol. Chem. 250:1975;7771-7779.
    • (1975) J. Biol. Chem. , vol.250 , pp. 7771-7779
    • Pacaud, M.1    Richaud, C.2
  • 4
    • 0024599588 scopus 로고
    • Dipeptidylpeptidase IV and trypsin-like enzymatic degradation of human growth hormone-releasing hormone in plasma
    • Frohman L.A., Downs T.R., Heimer E.P., Felix A.M. Dipeptidylpeptidase IV and trypsin-like enzymatic degradation of human growth hormone-releasing hormone in plasma. J. Clin. Invest. 83:1989;1533-1540.
    • (1989) J. Clin. Invest. , vol.83 , pp. 1533-1540
    • Frohman, L.A.1    Downs, T.R.2    Heimer, E.P.3    Felix, A.M.4
  • 5
    • 0024461040 scopus 로고
    • The primary structure of porcine liver acylamino acid-releasing enzyme deduced from cDNA sequences
    • Mitta M., Asada K., Uchimura Y., Kimizuka F., Kato I., Sakiyama F., Tsunasawa S. The primary structure of porcine liver acylamino acid-releasing enzyme deduced from cDNA sequences. J. Biochem. 106:1989;548-551.
    • (1989) J. Biochem. , vol.106 , pp. 548-551
    • Mitta, M.1    Asada, K.2    Uchimura, Y.3    Kimizuka, F.4    Kato, I.5    Sakiyama, F.6    Tsunasawa, S.7
  • 6
    • 0036178438 scopus 로고    scopus 로고
    • The prolyl oligopeptidase family
    • Polgar L. The prolyl oligopeptidase family. Cell Mol. Life Sci. 59:2002;349-362.
    • (2002) Cell Mol. Life Sci. , vol.59 , pp. 349-362
    • Polgar, L.1
  • 7
    • 0025912444 scopus 로고
    • Triggering of the proteinase dipeptidyl peptidase IV(CD26) amplifies human T lymphocyte proliferation
    • Bednarczyk J.L., Carroll S.M., Marin C., McIntyre B.W. Triggering of the proteinase dipeptidyl peptidase IV(CD26) amplifies human T lymphocyte proliferation. J. Cell. Biochem. 46:1991;206-218.
    • (1991) J. Cell. Biochem. , vol.46 , pp. 206-218
    • Bednarczyk, J.L.1    Carroll, S.M.2    Marin, C.3    McIntyre, B.W.4
  • 9
    • 0001095690 scopus 로고    scopus 로고
    • Reduced postprandial concentrations of intact biologically active glucagon-like peptide 1 in type 2 diabetic patients
    • Vilsboll T., Krarup T., Deacon C.F., Madsbad S., Holst J.J. Reduced postprandial concentrations of intact biologically active glucagon-like peptide 1 in type 2 diabetic patients. Diabetes. 50:2001;609-613.
    • (2001) Diabetes , vol.50 , pp. 609-613
    • Vilsboll, T.1    Krarup, T.2    Deacon, C.F.3    Madsbad, S.4    Holst, J.J.5
  • 10
    • 0034648026 scopus 로고    scopus 로고
    • The HIV-1 gp120 inhibits the binding of adenosine deaminase to CD26 by a mechanism modulated by CD4 and CXCR4 expression
    • Blanco J., Valenzuela A., Herrera C., Lluis C., Hovanessian A.G., Franco R. The HIV-1 gp120 inhibits the binding of adenosine deaminase to CD26 by a mechanism modulated by CD4 and CXCR4 expression. FEBS Lett. 477:2000;123-128.
    • (2000) FEBS Lett. , vol.477 , pp. 123-128
    • Blanco, J.1    Valenzuela, A.2    Herrera, C.3    Lluis, C.4    Hovanessian, A.G.5    Franco, R.6
  • 11
    • 0032563162 scopus 로고    scopus 로고
    • Prolyl oligopeptidase: An unusual β-propeller domain regulates proteolysis
    • Fulop V., Bocskei Z., Polgar L. Prolyl oligopeptidase: an unusual β-propeller domain regulates proteolysis. Cell. 94:1998;161-170.
    • (1998) Cell , vol.94 , pp. 161-170
    • Fulop, V.1    Bocskei, Z.2    Polgar, L.3
  • 12
    • 0242558716 scopus 로고    scopus 로고
    • β-Propellers: Structural rigidity and functional diversity
    • Fulop V., Jones D.T. β-Propellers: structural rigidity and functional diversity. Curr. Opin. Struct. Biol. 9:1999;715-721.
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 715-721
    • Fulop, V.1    Jones, D.T.2
  • 13
    • 0034993094 scopus 로고    scopus 로고
    • Protein folds propelled by diversity
    • Paoli M. Protein folds propelled by diversity. Prog. Biophys. Mol. Biol. 76:2001;103-130.
    • (2001) Prog. Biophys. Mol. Biol. , vol.76 , pp. 103-130
    • Paoli, M.1
  • 14
    • 0036226347 scopus 로고    scopus 로고
    • Novel sequences propel familiar folds
    • Jawad Z., Paoli M. Novel sequences propel familiar folds. Structure. 10:2002;447-454.
    • (2002) Structure , vol.10 , pp. 447-454
    • Jawad, Z.1    Paoli, M.2
  • 17
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4. The CCP4 suite: programs for protein crystallography, Acta Crystallogr. D 50 (1994) 760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 18
    • 0002634621 scopus 로고
    • Maximum likelihood refinement of heavy atom parameters
    • W. Wolf, P.R. Evans, & A.G.W. Leslie. Warrington, UK: Science and Engineering Research Council/Daresbury Laboratory
    • Otwinowski Z. Maximum likelihood refinement of heavy atom parameters. Wolf W., Evans P.R., Leslie A.G.W. Isomorphous Replacement and Anomalous Scattering. 1991;80-86 Science and Engineering Research Council/Daresbury Laboratory, Warrington, UK.
    • (1991) Isomorphous Replacement and Anomalous Scattering , pp. 80-86
    • Otwinowski, Z.1
  • 21
    • 85031212497 scopus 로고
    • Isolation and characterization of dipeptidyl peptidase IV from human placenta
    • Puschel G., Mentlein R., Heymann E. Isolation and characterization of dipeptidyl peptidase IV from human placenta. Biochem. J. 262:1989;327-334.
    • (1989) Biochem. J. , vol.262 , pp. 327-334
    • Puschel, G.1    Mentlein, R.2    Heymann, E.3
  • 22
    • 0034650563 scopus 로고    scopus 로고
    • The structure of TolB, an essential component of the tol-dependent translocation system, and its protein-protein interaction with the translocation domain of colicin E9
    • Carr S., Penfold C.N., Bamford V., James R., Hemmings A.M. The structure of TolB, an essential component of the tol-dependent translocation system, and its protein-protein interaction with the translocation domain of colicin E9. Structure. 8:2000;57-66.
    • (2000) Structure , vol.8 , pp. 57-66
    • Carr, S.1    Penfold, C.N.2    Bamford, V.3    James, R.4    Hemmings, A.M.5
  • 23
    • 0000038304 scopus 로고    scopus 로고
    • Binding to human dipeptidyl peptidase IV by adenosine deaminase and antibodies that inhibit ligand binding involves overlapping, discontinuous sites on a predicted β propeller domain
    • Abbott C.A., McCaughan G.W., Levy M.T., Church W.B., Gorrell M.D. Binding to human dipeptidyl peptidase IV by adenosine deaminase and antibodies that inhibit ligand binding involves overlapping, discontinuous sites on a predicted β propeller domain. Eur. J. Biochem. 266:1999;798-810.
    • (1999) Eur. J. Biochem. , vol.266 , pp. 798-810
    • Abbott, C.A.1    McCaughan, G.W.2    Levy, M.T.3    Church, W.B.4    Gorrell, M.D.5
  • 24
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:1994;4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 25
    • 0034279642 scopus 로고    scopus 로고
    • Catalysis of serine oligopeptidases is controlled by a gating filter mechanism
    • Fulop V., Szeltner Z., Polgar L. Catalysis of serine oligopeptidases is controlled by a gating filter mechanism. EMBO Rep. 1:2000;277-281.
    • (2000) EMBO Rep. , vol.1 , pp. 277-281
    • Fulop, V.1    Szeltner, Z.2    Polgar, L.3
  • 26
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of proteins
    • Kraulis P. MOLSCRIPT: a program to produce both detailed and schematic plots of proteins. J. Appl. Cryst. 24:1991;946-950.
    • (1991) J. Appl. Cryst. , vol.24 , pp. 946-950
    • Kraulis, P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.