메뉴 건너뛰기




Volumn 8, Issue 10, 1999, Pages 1930-1945

Allosteric inhibition of glycogen phosphorylase α by the potential antidiabetic drug 3-isopropyl 4-(2-chlorophenyl)-1,4-dihydro-1-ethyl-2- methyl-pyridine-3,5,6-tricarboxylate

Author keywords

Allosteric site; Crystal structure; Diabetes; Glycogen metabolism; Inhibition; Phosphorylase

Indexed keywords

3 ISOPROPYL 4 (2 CHLOROPHENYL) 1,4 DIHYDRO 1 ETHYL 2 METHYLPYRIDINE 3,5,6 TRICARBOXYLIC ACID; CARBOXYLIC ACID DERIVATIVE; GLUCOSE; GLUCOSE 1 PHOSPHATE; GLYCOGEN; GLYCOGEN PHOSPHORYLASE; SERINE; UNCLASSIFIED DRUG;

EID: 0032882213     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.8.10.1930     Document Type: Article
Times cited : (46)

References (38)
  • 1
    • 0026033985 scopus 로고
    • Structural mechanism for glycogen phosphorylase control by phosphorylation and AMP
    • Barford D, Hu SH, Johnson LN. 1991. Structural mechanism for glycogen phosphorylase control by phosphorylation and AMP. J Mol Biol 218:233-260.
    • (1991) J Mol Biol , vol.218 , pp. 233-260
    • Barford, D.1    Hu, S.H.2    Johnson, L.N.3
  • 2
    • 0024322304 scopus 로고
    • The allosteric transition of glycogen phosphorylase
    • Barford D, Johnson LN. 1989. The allosteric transition of glycogen phosphorylase. Nature 340:609-616.
    • (1989) Nature , vol.340 , pp. 609-616
    • Barford, D.1    Johnson, L.N.2
  • 3
    • 0026695872 scopus 로고
    • The structure, role, and regulation of type-1 protein phosphatases
    • Bollen M, Stalmans W. 1992. The structure, role, and regulation of type-1 protein phosphatases. Crit Rev Biochem Mol Biol 27:227-281.
    • (1992) Crit Rev Biochem Mol Biol , vol.27 , pp. 227-281
    • Bollen, M.1    Stalmans, W.2
  • 5
    • 0037877123 scopus 로고    scopus 로고
    • New Haven, CT: Department of Molecular Biophysics and Biochemistry, Yale University
    • Brünger AT. 1996. X-PLOR version 3.8. New Haven, CT: Department of Molecular Biophysics and Biochemistry, Yale University.
    • (1996) X-PLOR Version 3.8
    • Brünger, A.T.1
  • 6
    • 0015912123 scopus 로고
    • The subunit structure of rabbit-skeletal-muscle phosphorylase kinase, and the molecular basis of its activation reactions
    • Cohen P. 1973. The subunit structure of rabbit-skeletal-muscle phosphorylase kinase, and the molecular basis of its activation reactions. Eur J Biochem 34:1-14.
    • (1973) Eur J Biochem , vol.34 , pp. 1-14
    • Cohen, P.1
  • 7
    • 0028103275 scopus 로고
    • The CCP4 Suite: Programs for protein crystallography
    • (Collaborative Computational Project, Number 4). 1994. The CCP4 Suite: Programs for protein crystallography. Acta Crystallogr D 50:760-763.
    • (1994) Acta Crystallogr D , vol.50 , pp. 760-763
  • 9
    • 0018867079 scopus 로고
    • The structures and related functions of phosphorylase a
    • Fletterick RJ, Madsen NB. 1980. The structures and related functions of phosphorylase a. Ann Rev Biochem 49:31-61.
    • (1980) Ann Rev Biochem , vol.49 , pp. 31-61
    • Fletterick, R.J.1    Madsen, N.B.2
  • 10
    • 0017226279 scopus 로고
    • Low-resolution structure of the glycogen phosphorylase a monomer and comparison with phosphorylase b
    • Fletterick RJ, Sygusch J, Murray N, Madsen NB, Johnson LN. 1976. Low-resolution structure of the glycogen phosphorylase a monomer and comparison with phosphorylase b. J Mol Biol 103:1-13.
    • (1976) J Mol Biol , vol.103 , pp. 1-13
    • Fletterick, R.J.1    Sygusch, J.2    Murray, N.3    Madsen, N.B.4    Johnson, L.N.5
  • 11
    • 0031956876 scopus 로고    scopus 로고
    • The structure of a glycogen phosphorylase spirohydantoin complex at 1.8 À resolution and 100 K: The role of the water structure and its contribution to binding
    • Gregoriou M, Noble MEM, Watson KA, Garman EF, Krulle TM, Fuente C, Fleet GWJ, Oikonomakos NG, Johnson LN. 1998. The structure of a glycogen phosphorylase spirohydantoin complex at 1.8 À resolution and 100 K: The role of the water structure and its contribution to binding. Protein Sci 7:915-927.
    • (1998) Protein Sci , vol.7 , pp. 915-927
    • Gregoriou, M.1    Noble, M.E.M.2    Watson, K.A.3    Garman, E.F.4    Krulle, T.M.5    Fuente, C.6    Fleet, G.W.J.7    Oikonomakos, N.G.8    Johnson, L.N.9
  • 12
    • 78651151913 scopus 로고
    • The role of adenylic acid in the activity of phosphorylase
    • Helmreich EJM, Cori CF. 1964. The role of adenylic acid in the activity of phosphorylase. Proc Natl Acad Sci USA 57:131-138.
    • (1964) Proc Natl Acad Sci USA , vol.57 , pp. 131-138
    • Helmreich, E.J.M.1    Cori, C.F.2
  • 13
    • 0026562948 scopus 로고
    • Glycogen phosphorylase: Control by phosphorylation and allosteric effectors
    • Johnson LN. 1992. Glycogen phosphorylase: Control by phosphorylation and allosteric effectors. FASEB J 6:2274-2282.
    • (1992) FASEB J , vol.6 , pp. 2274-2282
    • Johnson, L.N.1
  • 15
    • 0027236184 scopus 로고
    • The refined crystal structure of the glycogen phosphorylase-glucose 6-phosphate complex
    • Johnson LN, Martin JL, Acharya KR, Barford D, Oikonomakos NG. 1993. The refined crystal structure of the glycogen phosphorylase-glucose 6-phosphate complex. J Mol Biol 232:253-267.
    • (1993) J Mol Biol , vol.232 , pp. 253-267
    • Johnson, L.N.1    Martin, J.L.2    Acharya, K.R.3    Barford, D.4    Oikonomakos, N.G.5
  • 16
    • 84889120137 scopus 로고
    • Improved methods for the building of protein models in electron density maps and the location of errors in these models
    • Jones TA, Zou JY, Cowan SW, Kjeldgaard M. 1991. Improved methods for the building of protein models in electron density maps and the location of errors in these models. Acta Crystallogr A47:110-119.
    • (1991) Acta Crystallogr A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 17
    • 0014344064 scopus 로고
    • Subunit interactions and their relationship to the allosteric properties of rabbit skeletal muscle phosphorylase b
    • Kastenschmidt LL, Kastenschmidt J, Helmreich EJM. 1968. Subunit interactions and their relationship to the allosteric properties of rabbit skeletal muscle phosphorylase b. Biochemistry 7:3590-3608.
    • (1968) Biochemistry , vol.7 , pp. 3590-3608
    • Kastenschmidt, L.L.1    Kastenschmidt, J.2    Helmreich, E.J.M.3
  • 18
    • 0018243091 scopus 로고
    • Synergistic regulation of phosphorylase a by glucose and caffeine
    • Kasvinsky PJ, Shechosky S, Fletterick RJ. 1978. Synergistic regulation of phosphorylase a by glucose and caffeine. J Biol Chem 253:9102-9106.
    • (1978) J Biol Chem , vol.253 , pp. 9102-9106
    • Kasvinsky, P.J.1    Shechosky, S.2    Fletterick, R.J.3
  • 19
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski RA, MacArthur MW, Moss DS, Thorton JM. 1993. PROCHECK: A program to check the stereochemical quality of protein structures. J Appl Cryst 26:283-291.
    • (1993) J Appl Cryst , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thorton, J.M.4
  • 20
    • 0342446207 scopus 로고
    • Glycogen phosphorylase
    • Boyer PD, Krebs EG, eds. New York: Academic Press.
    • Madsen NB. 1986. Glycogen phosphorylase. In: Boyer PD, Krebs EG, eds. The enzymes, 3rd ed., vol 17. New York: Academic Press. pp 366-394.
    • (1986) The Enzymes, 3rd Ed. , vol.17 , pp. 366-394
    • Madsen, N.B.1
  • 23
    • 0020525283 scopus 로고
    • Effect of glucose-6-P on the catalytic and structural properties of glycogen phosphorylase
    • Melpidou AE, Oikonomakos NG. 1983. Effect of glucose-6-P on the catalytic and structural properties of glycogen phosphorylase. FEBS Lett 154: 105-110.
    • (1983) FEBS Lett , vol.154 , pp. 105-110
    • Melpidou, A.E.1    Oikonomakos, N.G.2
  • 24
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: A plausible model
    • Monod J, Changeux JP, Jacob F. 1965. On the nature of allosteric transitions: A plausible model. J Mol Biol 12:88-118.
    • (1965) J Mol Biol , vol.12 , pp. 88-118
    • Monod, J.1    Changeux, J.P.2    Jacob, F.3
  • 25
    • 0002231480 scopus 로고
    • Rabbit muscle glycogen phosphorylase b: Structural basis of activation and catalysis
    • Harding JJ, Crabbe MJC, eds. Boca Raton, FL: CRC Press.
    • Oikonomakos NG, Acharya KR, Johnson LN. 1992. Rabbit muscle glycogen phosphorylase b: Structural basis of activation and catalysis. In: Harding JJ, Crabbe MJC, eds. Post-translational modification of proteins. Boca Raton, FL: CRC Press. pp 81-151.
    • (1992) Post-translational Modification of Proteins , pp. 81-151
    • Oikonomakos, N.G.1    Acharya, K.R.2    Johnson, L.N.3
  • 27
    • 0029416953 scopus 로고
    • The binding of 2-deoxy-glucose-6-phosphate to glycogen phosphorylase b: Kinetic and crystallographic studies
    • Oikonomakos NG, Zographos SE, Johnson LN, Papageorgiou AC, Acharya KR. 1995b. The binding of 2-deoxy-glucose-6-phosphate to glycogen phosphorylase b: Kinetic and crystallographic studies. J Mol Biol 254:900-917.
    • (1995) J Mol Biol , vol.254 , pp. 900-917
    • Oikonomakos, N.G.1    Zographos, S.E.2    Johnson, L.N.3    Papageorgiou, A.C.4    Acharya, K.R.5
  • 29
    • 0028918780 scopus 로고
    • Expression, purification and crystallization of phosphorylase kinase catalytic domain
    • Owen DJ, Papageorgiou AC, Garman EF, Noble MEM, Johnson LN. 1995. Expression, purification and crystallization of phosphorylase kinase catalytic domain. J Mol Biol 246:374-381.
    • (1995) J Mol Biol , vol.246 , pp. 374-381
    • Owen, D.J.1    Papageorgiou, A.C.2    Garman, E.F.3    Noble, M.E.M.4    Johnson, L.N.5
  • 30
    • 84944812409 scopus 로고
    • Improved Fourier coefficients for maps using phases from partial structures with errors
    • Read RJ. 1986. Improved Fourier coefficients for maps using phases from partial structures with errors. Acta Crystallogr A 42:140-149.
    • (1986) Acta Crystallogr A , vol.42 , pp. 140-149
    • Read, R.J.1
  • 31
    • 0003518480 scopus 로고
    • New York: Wiley Interscience
    • Segel IH. 1975. Enzyme kinetics. New York: Wiley Interscience. pp 465-504.
    • (1975) Enzyme Kinetics , pp. 465-504
    • Segel, I.H.1
  • 33
    • 0023176374 scopus 로고
    • Structure of the nucleotide activation switch in glycogen phosphorylase a
    • Sprang SR, Goldsmith E, Fletterick R. 1987. Structure of the nucleotide activation switch in glycogen phosphorylase a. Science 237:1012-1019.
    • (1987) Science , vol.237 , pp. 1012-1019
    • Sprang, S.R.1    Goldsmith, E.2    Fletterick, R.3
  • 34
    • 0020481297 scopus 로고
    • Catalytic site of glycogen phosphorylase: Structure of the T state and specificity for α-D-glucose
    • Sprang SR, Goldsmith HJ, Fletterick RJ, Withers SG, Madsen NB. 1982. Catalytic site of glycogen phosphorylase: Structure of the T state and specificity for α-D-glucose. Biochemistry 21:5364-5371.
    • (1982) Biochemistry , vol.21 , pp. 5364-5371
    • Sprang, S.R.1    Goldsmith, H.J.2    Fletterick, R.J.3    Withers, S.G.4    Madsen, N.B.5
  • 35
    • 0026326962 scopus 로고
    • Structural basis for activation of glycogen phosphorylase b by adenosine monophosphate
    • Sprang SR, Withers SG, Goldsmith EJ, Fletterick RJ, Madsen NB. 1991. Structural basis for activation of glycogen phosphorylase b by adenosine monophosphate. Science 254:1367-1371.
    • (1991) Science , vol.254 , pp. 1367-1371
    • Sprang, S.R.1    Withers, S.G.2    Goldsmith, E.J.3    Fletterick, R.J.4    Madsen, N.B.5
  • 36
    • 0022996027 scopus 로고
    • Hydrogen bonding and specificity. Fluorodeoxy sugars as probes of hydrogen bonding in the glycogen phosphorylase-glucose complex
    • Street IP, Armstrong CR, Withers SG. 1986. Hydrogen bonding and specificity. Fluorodeoxy sugars as probes of hydrogen bonding in the glycogen phosphorylase-glucose complex. Biochemistry 25:6021-6027.
    • (1986) Biochemistry , vol.25 , pp. 6021-6027
    • Street, I.P.1    Armstrong, C.R.2    Withers, S.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.