메뉴 건너뛰기




Volumn 48, Issue 9, 1999, Pages 1698-1705

Structural model of human glucokinase in complex with glucose and ATP: Implications for the mutants that cause hypo- and hyperglycemia

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE MAGNESIUM; ENZYME ACTIVATOR; ENZYME INHIBITOR; GLUCOKINASE; GLUCOSE; HEXOKINASE; MUTANT PROTEIN;

EID: 0032880513     PISSN: 00121797     EISSN: None     Source Type: Journal    
DOI: 10.2337/diabetes.48.9.1698     Document Type: Article
Times cited : (63)

References (34)
  • 2
    • 0025334163 scopus 로고
    • Glucokinase as glucose sensor and metabolic signal generator in pancreatic beta-cells and hepatocytes
    • Matschinsky FM: Glucokinase as glucose sensor and metabolic signal generator in pancreatic beta-cells and hepatocytes. Diabetes 39:647-652, 1990
    • (1990) Diabetes , vol.39 , pp. 647-652
    • Matschinsky, F.M.1
  • 3
    • 0026520193 scopus 로고
    • Molecular physiology of the regulation of hepatic gluconeogenesis and glycolysis
    • Pilkis SJ, Granner DK: Molecular physiology of the regulation of hepatic gluconeogenesis and glycolysis. Ann Rev Physiol 54:885-909, 1992
    • (1992) Ann Rev Physiol , vol.54 , pp. 885-909
    • Pilkis, S.J.1    Granner, D.K.2
  • 8
    • 0028015892 scopus 로고
    • Glucokinase: Structural analysis of a protein involved in susceptibility to diabetes
    • Pilkis SJ, Weber IT, Harrison RW, Bell GI: Glucokinase: structural analysis of a protein involved in susceptibility to diabetes. J Biol Chem 269:21925-21928, 1994
    • (1994) J Biol Chem , vol.269 , pp. 21925-21928
    • Pilkis, S.J.1    Weber, I.T.2    Harrison, R.W.3    Bell, G.I.4
  • 9
    • 0029034723 scopus 로고
    • Variable effects of maturity onset diabetes of youth (MODY)-associated glucokinase mutations on substrate interactions and stability of the enzyme
    • Liang Y, Kesavan P, Wang LQ, Niswender K, Tanizawa Y, Permutt MA, Magnuson MA, Matschinsky FM: Variable effects of maturity onset diabetes of youth (MODY)-associated glucokinase mutations on substrate interactions and stability of the enzyme. Biochem J 309:167-173, 1995
    • (1995) Biochem J , vol.309 , pp. 167-173
    • Liang, Y.1    Kesavan, P.2    Wang, L.Q.3    Niswender, K.4    Tanizawa, Y.5    Permutt, M.A.6    Magnuson, M.A.7    Matschinsky, F.M.8
  • 11
    • 0032875616 scopus 로고    scopus 로고
    • Mutants of glucokinase cause hypo- and hyperglycemia syndromes and their analysis illuminates fundamental quantitative concepts of glucose homeostasis
    • In press
    • Davis E, Cuesta-Munoz A, Raoul M, Buettger C, Sweet I, Moates M, Magnuson MA, Matschinsky FM: Mutants of glucokinase cause hypo- and hyperglycemia syndromes and their analysis illuminates fundamental quantitative concepts of glucose homeostasis. Diabetologia. In press
    • Diabetologia
    • Davis, E.1    Cuesta-Munoz, A.2    Raoul, M.3    Buettger, C.4    Sweet, I.5    Moates, M.6    Magnuson, M.A.7    Matschinsky, F.M.8
  • 12
    • 0342526544 scopus 로고
    • Molecular model of human β-cell glucokinase built by analogy to the crystal structure of yeast hexokinase B
    • St. Charles R, Harrison RW, Bell GI, Pilkis SJ, Weber IT: Molecular model of human β-cell glucokinase built by analogy to the crystal structure of yeast hexokinase B. Diabetes 43:784-791, 1994
    • (1994) Diabetes , vol.43 , pp. 784-791
    • St. Charles, R.1    Harrison, R.W.2    Bell, G.I.3    Pilkis, S.J.4    Weber, I.T.5
  • 13
    • 0027970547 scopus 로고
    • Site-directed mutagenesis studies on the determinants of sugar specificity and cooperative behavior of human β-cell glucokinase
    • Xu LZ, Zhang W, Weber IT, Harrison RW, Pilkis SJ: Site-directed mutagenesis studies on the determinants of sugar specificity and cooperative behavior of human β-cell glucokinase. J Biol Chem 269:27458-27465, 1994
    • (1994) J Biol Chem , vol.269 , pp. 27458-27465
    • Xu, L.Z.1    Zhang, W.2    Weber, I.T.3    Harrison, R.W.4    Pilkis, S.J.5
  • 14
    • 0029009275 scopus 로고
    • Sugar specificity of human β-cell glucokinase: Correlation of molecular models with kinetic measurements
    • Xu LZ, Weber IT, Harrison RW, Gidh-Jain M, Pilkis SJ: Sugar specificity of human β-cell glucokinase: correlation of molecular models with kinetic measurements. Biochem 34:6083-6092, 1995
    • (1995) Biochem , vol.34 , pp. 6083-6092
    • Xu, L.Z.1    Weber, I.T.2    Harrison, R.W.3    Gidh-Jain, M.4    Pilkis, S.J.5
  • 16
    • 0017807667 scopus 로고
    • Sequencing of a protein by X-ray crystallography. I. Interpretation of yeast hexokinase B at 2.5Å resolution by model building
    • Anderson CM, McDonald RC, Steitz TA: Sequencing of a protein by X-ray crystallography. I. Interpretation of yeast hexokinase B at 2.5Å resolution by model building. J Mol Biol 123:1-13, 1978
    • (1978) J Mol Biol , vol.123 , pp. 1-13
    • Anderson, C.M.1    McDonald, R.C.2    Steitz, T.A.3
  • 17
    • 0019201173 scopus 로고
    • Structure of a complex between yeast hexokinase A and glucose. II. Detailed comparisons of confomiational and active site configuration with the native hexokinase B monomer and dimer
    • Bennett WS, Steitz TA: Structure of a complex between yeast hexokinase A and glucose. II. Detailed comparisons of confomiational and active site configuration with the native hexokinase B monomer and dimer. J Mol Biol 140:211-221, 1980
    • (1980) J Mol Biol , vol.140 , pp. 211-221
    • Bennett, W.S.1    Steitz, T.A.2
  • 18
  • 19
    • 0032518372 scopus 로고    scopus 로고
    • Crystal structure of recombinant human brain hexokinase complexed with glucose and glucose-6-phosphate
    • Aleshin AE, Zeng C, Bourenkov GP, Bartunik HD, Fromm HJ, Honzatko RB: Crystal structure of recombinant human brain hexokinase complexed with glucose and glucose-6-phosphate. Structure 6:39-50, 1998
    • (1998) Structure , vol.6 , pp. 39-50
    • Aleshin, A.E.1    Zeng, C.2    Bourenkov, G.P.3    Bartunik, H.D.4    Fromm, H.J.5    Honzatko, R.B.6
  • 20
    • 0032544488 scopus 로고    scopus 로고
    • Regulation of hexokinase I: Crystal structure of recombinant human brain hexokinase complexed with glucose and phosphate
    • Aleshin AE, Zeng C, Bartunik HD, Fromm HJ, Honzatko RB: Regulation of hexokinase I: crystal structure of recombinant human brain hexokinase complexed with glucose and phosphate. J Mol Biol 282:345-357, 1998
    • (1998) J Mol Biol , vol.282 , pp. 345-357
    • Aleshin, A.E.1    Zeng, C.2    Bartunik, H.D.3    Fromm, H.J.4    Honzatko, R.B.5
  • 21
    • 0001048849 scopus 로고
    • Stiffness and energy conservation in the molecular dynamics: An improved integrator
    • Harrison RW: Stiffness and energy conservation in the molecular dynamics: an improved integrator. J Comp Chem 14:1112-1122, 1993
    • (1993) J Comp Chem , vol.14 , pp. 1112-1122
    • Harrison, R.W.1
  • 22
    • 0030685159 scopus 로고    scopus 로고
    • Molecular mechanics calculations on Rous sarcoma virus protease with peptide substrates
    • Weber IT, Harrison RW: Molecular mechanics calculations on Rous sarcoma virus protease with peptide substrates. Protein Sci 6:2365-2374, 1997
    • (1997) Protein Sci , vol.6 , pp. 2365-2374
    • Weber, I.T.1    Harrison, R.W.2
  • 23
    • 0029587028 scopus 로고
    • Analysis of six protein structures predicted by comparative modeling techniques
    • Harrison RW, Chatterjee D, Weber IT Analysis of six protein structures predicted by comparative modeling techniques. Proteins Struct Funct Genet 23:463-471, 1995
    • (1995) Proteins Struct Funct Genet , vol.23 , pp. 463-471
    • Harrison, R.W.1    Chatterjee, D.2    Weber, I.T.3
  • 24
    • 0029848096 scopus 로고    scopus 로고
    • Site-directed mutagenesis and modeling of the putative ATP-binding domain of human brain hexokinase
    • Zeng C, Aleshin AE, Harrison RW, Fromm HJ: Site-directed mutagenesis and modeling of the putative ATP-binding domain of human brain hexokinase. Biochem 35:13157-13164, 1996
    • (1996) Biochem , vol.35 , pp. 13157-13164
    • Zeng, C.1    Aleshin, A.E.2    Harrison, R.W.3    Fromm, H.J.4
  • 25
    • 0032527132 scopus 로고    scopus 로고
    • Bovine F1-ATPase covalently inhibited with 4-chloro-7-nitrobenzofurazan: The structure provides further support for a rotary catalytic mechanism
    • Orriss GL, Leslie AG, Braig K, Walker JE: Bovine F1-ATPase covalently inhibited with 4-chloro-7-nitrobenzofurazan: the structure provides further support for a rotary catalytic mechanism. Structure 6:831-837, 1998
    • (1998) Structure , vol.6 , pp. 831-837
    • Orriss, G.L.1    Leslie, A.G.2    Braig, K.3    Walker, J.E.4
  • 26
    • 0000082544 scopus 로고
    • CHAIN: A crystallographic modeling program
    • Sack JS: CHAIN: a crystallographic modeling program. J Mol Graphics 6: 224-225, 1988
    • (1988) J Mol Graphics , vol.6 , pp. 224-225
    • Sack, J.S.1
  • 27
    • 0031050536 scopus 로고    scopus 로고
    • Structural instability of mutant beta-cell glucokinase: Implications for the molecular pathogenesis of maturity-onset diabetes of the young (type-2)
    • Kesavan P, Wang L, Davis E, Cuesta A, Sweet I, Niswender K, Magnuson MA, Matschinsky FM: Structural instability of mutant beta-cell glucokinase: implications for the molecular pathogenesis of maturity-onset diabetes of the young (type-2). Biochem J 322:57-63, 1997
    • (1997) Biochem J , vol.322 , pp. 57-63
    • Kesavan, P.1    Wang, L.2    Davis, E.3    Cuesta, A.4    Sweet, I.5    Niswender, K.6    Magnuson, M.A.7    Matschinsky, F.M.8
  • 28
    • 0027485083 scopus 로고
    • Comparison of conformational characteristics in structurally similar protein pairs
    • Flores TP, Orengo CA, Moss DS, Thornton JM: Comparison of conformational characteristics in structurally similar protein pairs. Prot Sci 2: 1811-1826, 1993
    • (1993) Prot Sci , vol.2 , pp. 1811-1826
    • Flores, T.P.1    Orengo, C.A.2    Moss, D.S.3    Thornton, J.M.4
  • 29
    • 0025270076 scopus 로고
    • Evaluation of homology modeling of HIV protease
    • Weber IT: Evaluation of homology modeling of HIV protease. Proteins Struct Funct Genet 7:172-184, 1990
    • (1990) Proteins Struct Funct Genet , vol.7 , pp. 172-184
    • Weber, I.T.1
  • 30
    • 0029653395 scopus 로고
    • Human β-cell glucokinase: Dual role of Ser-151 in catalysis and hexose affinity
    • Xu LZ, Harrison RW, Weber IT, Pilkis SJ: Human β-cell glucokinase: dual role of Ser-151 in catalysis and hexose affinity. J Biol Chem 270:9939-9646, 1995
    • (1995) J Biol Chem , vol.270 , pp. 9939-19646
    • Xu, L.Z.1    Harrison, R.W.2    Weber, I.T.3    Pilkis, S.J.4
  • 31
    • 0031984519 scopus 로고    scopus 로고
    • The roles of glycines residues in the ATP binding site of human brain hexokinase
    • Zeng C, Aleshin A, Chen G, Honzatko RB, Fromm HJ: The roles of glycines residues in the ATP binding site of human brain hexokinase. J Biol Chem 273:700-704, 1998
    • (1998) J Biol Chem , vol.273 , pp. 700-704
    • Zeng, C.1    Aleshin, A.2    Chen, G.3    Honzatko, R.B.4    Fromm, H.J.5
  • 34
    • 0029918678 scopus 로고    scopus 로고
    • Amino acid conservation in animal glucokinases: Identification of residues implicated in the interaction with the regulatory protein
    • Veiga-da-Cunha M, Courtois S, Michel A, Gosselain E, Van Schattingen E: Amino acid conservation in animal glucokinases: identification of residues implicated in the interaction with the regulatory protein. J Biol Chem 271:6292-6297, 1996
    • (1996) J Biol Chem , vol.271 , pp. 6292-6297
    • Veiga-Da-Cunha, M.1    Courtois, S.2    Michel, A.3    Gosselain, E.4    Van Schattingen, E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.