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Volumn 284, Issue 2, 1998, Pages 477-488

The relationship between insulin bioactivity and structure in the NH2-terminal A-chain helix

Author keywords

Insulin A chain; Insulin mutant; Insulin receptor affinity; NMR; Solution structure

Indexed keywords

DRUG CARRIER; INSULIN; INSULIN RECEPTOR; MUTANT PROTEIN;

EID: 0032573528     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.2175     Document Type: Article
Times cited : (38)

References (40)
  • 6
    • 0018242265 scopus 로고
    • The chemical synthesis and biological evaluation of [1-L-alanine-A]- and [1-D-alanine-A]insulins
    • Cosmatos A., Cheng K., Okada Y., Katsoyannis P.G. The chemical synthesis and biological evaluation of [1-L-alanine-A]- and [1-D-alanine-A]insulins. J. Biol. Chem. 253:1978;6586-6590
    • (1978) J. Biol. Chem. , vol.253 , pp. 6586-6590
    • Cosmatos, A.1    Cheng, K.2    Okada, Y.3    Katsoyannis, P.G.4
  • 8
    • 0027934188 scopus 로고
    • Intra-A chain disulfide bond (A6-A11) of insulin is essential for displaying its activity
    • Dai Y., Tang J.-G. Intra-A chain disulfide bond (A6-A11) of insulin is essential for displaying its activity. Biochem. Mol. Biol. Int. 33:1994;1049-1053
    • (1994) Biochem. Mol. Biol. Int. , vol.33 , pp. 1049-1053
    • Dai, Y.1    Tang, J.-G.2
  • 9
    • 0030586703 scopus 로고    scopus 로고
    • Characteristic, activity and conformational studies of [A6-Ser,A11-Ser]-insulin
    • Dai Y., Tang J.-G. Characteristic, activity and conformational studies of [A6-Ser,A11-Ser]-insulin. Biomed. Biochem. Acta. 1296:1996;63-68
    • (1996) Biomed. Biochem. Acta , vol.1296 , pp. 63-68
    • Dai, Y.1    Tang, J.-G.2
  • 12
    • 0020365467 scopus 로고
    • Exchange of A1-glycine in bovine insulin with L - And D-tryptophan
    • Geiger R., Geisen K., Summ H.-D. Exchange of A1-glycine in bovine insulin with L - and D-tryptophan. Hoppe-Seyler's Z. Physiol. Chem. 363:1982;1231-1239
    • (1982) Hoppe-Seyler's Z. Physiol. Chem. , vol.363 , pp. 1231-1239
    • Geiger, R.1    Geisen, K.2    Summ, H.-D.3
  • 13
    • 0026549524 scopus 로고
    • Structure and dynamics of des-pentapeptide-insulin in solution: The molten-globule hypothesis
    • Hua Q.X., Kochoyan M., Weiss M.A. Structure and dynamics of des-pentapeptide-insulin in solution the molten-globule hypothesis. Proc. Natl Acad. Sci. USA. 89:1992;2379-2383
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 2379-2383
    • Hua, Q.X.1    Kochoyan, M.2    Weiss, M.A.3
  • 15
    • 0023643824 scopus 로고
    • Stereospecific assignments of side-chain protons and characterization of torsion angles in Eglin C
    • Hyberts S.G., Märki W., Wagner G. Stereospecific assignments of side-chain protons and characterization of torsion angles in Eglin C. Eur. J. Biochem. 164:1987;625-635
    • (1987) Eur. J. Biochem. , vol.164 , pp. 625-635
    • Hyberts, S.G.1    Märki, W.2    Wagner, G.3
  • 16
    • 0029986510 scopus 로고    scopus 로고
    • Solution structure of the superactive monomeric des-[Phe(B25)] human insulin mutant: Elucidation of the structural basis for the monomerization of des-[Phe(B25)] insulin and the dimerization of native insulin
    • Jørgensen A.M.M., Olsen H.B., Balschmidt P., Led J.J. Solution structure of the superactive monomeric des-[Phe(B25)] human insulin mutant elucidation of the structural basis for the monomerization of des-[Phe(B25)] insulin and the dimerization of native insulin. J. Mol. Biol. 257:1996;684-699
    • (1996) J. Mol. Biol , vol.257 , pp. 684-699
    • Jørgensen, A.M.M.1    Olsen, H.B.2    Balschmidt, P.3    Led, J.J.4
  • 17
    • 0029264937 scopus 로고
    • The high resolution solution structure of the insulin monomer determined by NMR
    • Kaarsholm N.C., Ludvigsen S. The high resolution solution structure of the insulin monomer determined by NMR. Receptor. 5:1995;1-8
    • (1995) Receptor , vol.5 , pp. 1-8
    • Kaarsholm, N.C.1    Ludvigsen, S.2
  • 18
    • 0024356816 scopus 로고
    • Comparison of solution structural flexibility and zinc binding domains for insulin, proinsulin, and miniproinsulin
    • Kaarsholm N.C., Ko H.-C., Dunn M.F. Comparison of solution structural flexibility and zinc binding domains for insulin, proinsulin, and miniproinsulin. Biochemistry. 28:1989;4427-4435
    • (1989) Biochemistry , vol.28 , pp. 4427-4435
    • Kaarsholm, N.C.1    Ko, H.-C.2    Dunn, M.F.3
  • 20
    • 0021289293 scopus 로고
    • Critical role of the A2 amino acid residue in the biological activity of insulin: [2-glycine-A]- and [2-alanine-A]insulins
    • Kitagawa K., Ogawa H., Burke G.T., Chanley J.D., Katsoyannis P.G. Critical role of the A2 amino acid residue in the biological activity of insulin [2-glycine-A]- and [2-alanine-A]insulins. Biochemistry. 23:1984;1405-1413
    • (1984) Biochemistry , vol.23 , pp. 1405-1413
    • Kitagawa, K.1    Ogawa, H.2    Burke, G.T.3    Chanley, J.D.4    Katsoyannis, P.G.5
  • 23
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi R., Billeter M., Wüthrich K. MOLMOL a program for display and analysis of macromolecular structures. J. Mol. Graphics. 14:1996;51-55
    • (1996) J. Mol. Graphics , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 24
    • 0026676167 scopus 로고
    • Sampling and efficiency of metric matrix distance geometry: A novel partial metrization algorithm
    • Kuszewski J., Nilges M., Brünger A.T. Sampling and efficiency of metric matrix distance geometry a novel partial metrization algorithm. J. Biomol. NMR. 2:1992;33-56
    • (1992) J. Biomol. NMR , vol.2 , pp. 33-56
    • Kuszewski, J.1    Nilges, M.2    Brünger, A.T.3
  • 25
    • 0028241787 scopus 로고
    • High resolution structure of an engineered biologically potent insulin monomer, B16 Tyr → His, as determined by nuclear magnetic resonance spectroscopy
    • Ludvigsen S., Roy M., Thøgersen H., Kaarsholm N.C. High resolution structure of an engineered biologically potent insulin monomer, B16 Tyr → His, as determined by nuclear magnetic resonance spectroscopy. Biochemistry. 33:1994;7998-8006
    • (1994) Biochemistry , vol.33 , pp. 7998-8006
    • Ludvigsen, S.1    Roy, M.2    Thøgersen, H.3    Kaarsholm, N.C.4
  • 26
    • 0032577326 scopus 로고    scopus 로고
    • A structural switch in a mutant insulin exposes key residues for receptor binding
    • Ludvigsen S., Olsen H.B., Kaarsholm N.C. A structural switch in a mutant insulin exposes key residues for receptor binding. J. Mol. Biol. 279:1998;1-7
    • (1998) J. Mol. Biol. , vol.279 , pp. 1-7
    • Ludvigsen, S.1    Olsen, H.B.2    Kaarsholm, N.C.3
  • 30
    • 0024553746 scopus 로고
    • Role of the phenylalanine B24 side-chain in directing insulin interaction with its receptor
    • Mirmira R.G., Tager H.S. Role of the phenylalanine B24 side-chain in directing insulin interaction with its receptor. J. Biol. Chem. 264:1989;6349-6354
    • (1989) J. Biol. Chem. , vol.264 , pp. 6349-6354
    • Mirmira, R.G.1    Tager, H.S.2
  • 31
    • 0025978173 scopus 로고
    • Importance of the character and configuration of residues B24, B25, and B26 in insulin-receptor interactions
    • Mirmira R.G., Nakagawa S.H., Tager H.S. Importance of the character and configuration of residues B24, B25, and B26 in insulin-receptor interactions. J. Biol. Chem. 266:1991;1428-1436
    • (1991) J. Biol. Chem. , vol.266 , pp. 1428-1436
    • Mirmira, R.G.1    Nakagawa, S.H.2    Tager, H.S.3
  • 33
    • 0022879089 scopus 로고
    • Role of the phenylalanine B25 side-chain in directing insulin interaction with its receptor
    • Nakagawa S.H., Tager H.S. Role of the phenylalanine B25 side-chain in directing insulin interaction with its receptor. J. Biol. Chem. 261:1986;7332-7341
    • (1986) J. Biol. Chem. , vol.261 , pp. 7332-7341
    • Nakagawa, S.H.1    Tager, H.S.2
  • 34
    • 0023645553 scopus 로고
    • Role of the COOH-terminal B-chain domain in insulin-receptor interactions
    • Nakagawa S.H., Tager H.S. Role of the COOH-terminal B-chain domain in insulin-receptor interactions. J. Biol. Chem. 262:1987;12054-12058
    • (1987) J. Biol. Chem. , vol.262 , pp. 12054-12058
    • Nakagawa, S.H.1    Tager, H.S.2
  • 35
    • 0026634650 scopus 로고
    • Importance of aliphatic side-chain structure at positions 2 and 3 of the insulin a chain in insulin-receptor interactions
    • Nakagawa S.H., Tager H.S. Importance of aliphatic side-chain structure at positions 2 and 3 of the insulin A chain in insulin-receptor interactions. Biochemistry. 31:1992;3204-3214
    • (1992) Biochemistry , vol.31 , pp. 3204-3214
    • Nakagawa, S.H.1    Tager, H.S.2
  • 36
    • 0024285896 scopus 로고
    • Determination of three-dimensional structures of proteins from interproton distance data by hybrid distance geometry-dynamical simulated annealing calculations
    • Nilges M., Clore G.M., Gronenborn A.M. Determination of three-dimensional structures of proteins from interproton distance data by hybrid distance geometry-dynamical simulated annealing calculations. FEBS Letters. 229:1988;317-324
    • (1988) FEBS Letters , vol.229 , pp. 317-324
    • Nilges, M.1    Clore, G.M.2    Gronenborn, A.M.3
  • 37
    • 0030015918 scopus 로고    scopus 로고
    • Solution structure of an engineered insulin monomer at neutral pH
    • Olsen H.B., Ludvigsen S., Kaarsholm N.C. Solution structure of an engineered insulin monomer at neutral pH. Biochemistry. 35:1996;8836-8845
    • (1996) Biochemistry , vol.35 , pp. 8836-8845
    • Olsen, H.B.1    Ludvigsen, S.2    Kaarsholm, N.C.3
  • 38
    • 0342559269 scopus 로고
    • [12-asparagine-B] human insulin. An analogue with modification in the hydrophobic core of insulin
    • Schwartz G.P., Burke G.T., Katsoyannis P.G. [12-asparagine-B] human insulin. An analogue with modification in the hydrophobic core of insulin. Int. J. Pept. Protein Res. 23:1981;394-401
    • (1981) Int. J. Pept. Protein Res. , vol.23 , pp. 394-401
    • Schwartz, G.P.1    Burke, G.T.2    Katsoyannis, P.G.3
  • 39
    • 0023645325 scopus 로고
    • Protein structures in solution by nuclear magnetic resonance and distance geometry the polypeptide fold of the basic pancreatic trypsin inhibitor determined using two different algorithms, DISGEO and DISMAN
    • Wagner G., Braun W., Havel T.F., Wüthrich K. Protein structures in solution by nuclear magnetic resonance and distance geometry the polypeptide fold of the basic pancreatic trypsin inhibitor determined using two different algorithms, DISGEO and DISMAN. J. Mol. Biol. 196:1987;611-639
    • (1987) J. Mol. Biol. , vol.196 , pp. 611-639
    • Wagner, G.1    Braun, W.2    Havel, T.F.3    Wüthrich, K.4
  • 40
    • 0026597879 scopus 로고
    • The chemical shift index: A fast and simple method for the assignment of protein secondary structure through NMR spectroscopy
    • Wishart D.S., Sykes B.D., Richards F.M. The chemical shift index a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. Biochemistry. 31:1992;1647-1651
    • (1992) Biochemistry , vol.31 , pp. 1647-1651
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.