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Volumn 107, Issue 5, 2010, Pages 1966-1970

Implications for the active form of human insulin based on the structural convergence of highly active hormone analogues

Author keywords

turn; Diabetes; Peptide bond isomerisation; Protein; Structure

Indexed keywords

AMINO ACID; INSULIN DERIVATIVE; INSULIN RECEPTOR;

EID: 76649083949     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0911785107     Document Type: Article
Times cited : (49)

References (34)
  • 1
    • 0000557482 scopus 로고
    • Structure of rhombohedral 2 zinc insulin crystals
    • Adams MJ, et al. (1969) Structure of rhombohedral 2 zinc insulin crystals. Nature, 224:491-495.
    • (1969) Nature , vol.224 , pp. 491-495
    • Adams, M.J.1
  • 2
    • 0025880180 scopus 로고
    • X-ray analysis of the single chain B29-A1 peptide-linked insulin molecule. a completely inactive analogue
    • Derewenda U, et al. (1991) X-ray analysis of the single chain B29-A1 peptide-linked insulin molecule. a completely inactive analogue. J Mol Biol, 220:425-433.
    • (1991) J Mol Biol , vol.220 , pp. 425-433
    • Derewenda, U.1
  • 3
    • 61349161850 scopus 로고    scopus 로고
    • Weiss MA (2009) Insulin and IGFs, ed Litwack G (Elsevier Academic, Inc, San Diego), pp 33-49.
    • Weiss MA (2009) Insulin and IGFs, ed Litwack G (Elsevier Academic, Inc, San Diego), pp 33-49.
  • 5
    • 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, Thogersen H, Kaarsholm NC (1994) High-resolution structure of an engineered biologically potent insulin monomer, B16 Tyr - - > His, as determined by nuclear magnetic resonance spectroscopy. Biochemistry, 33:7998-8006.
    • (1994) Biochemistry , vol.33 , pp. 7998-8006
    • Ludvigsen, S.1    Roy, M.2    Thogersen, H.3    Kaarsholm, N.C.4
  • 6
    • 37849047952 scopus 로고    scopus 로고
    • Structure of human insulin monomer in water/acetonitrile solution
    • Bocian W, et al. (2008) Structure of human insulin monomer in water/acetonitrile solution. J Biomol NMR, 40:55-64.
    • (2008) J Biomol NMR , vol.40 , pp. 55-64
    • Bocian, W.1
  • 7
    • 0025778802 scopus 로고
    • Comparative 2D NMR studies of human insulin and despentapeptide insulin: Sequential resonance assignment and implications for protein dynamics and receptor recognition
    • Hua QX, Weiss MA (1991) Comparative 2D NMR studies of human insulin and despentapeptide insulin: Sequential resonance assignment and implications for protein dynamics and receptor recognition. Biochemistry, 30:5505-5515.
    • (1991) Biochemistry , vol.30 , pp. 5505-5515
    • Hua, Q.X.1    Weiss, M.A.2
  • 8
    • 0025996911 scopus 로고
    • Receptor binding redefined by a structural switch in a mutant human insulin
    • Hua QX, Shoelson SE, Kochoyan M, Weiss MA (1991) Receptor binding redefined by a structural switch in a mutant human insulin. Nature, 354:238-241.
    • (1991) Nature , vol.354 , pp. 238-241
    • Hua, Q.X.1    Shoelson, S.E.2    Kochoyan, M.3    Weiss, M.A.4
  • 9
    • 0032577326 scopus 로고    scopus 로고
    • A structural switch in a mutant insulin exposes key residues for receptor binding
    • Ludvigsen S, Olsen HB, Kaarsholm NC (1998) A structural switch in a mutant insulin exposes key residues for receptor binding. J Mol Biol, 279:1-7.
    • (1998) J Mol Biol , vol.279 , pp. 1-7
    • Ludvigsen, S.1    Olsen, H.B.2    Kaarsholm, N.C.3
  • 10
    • 67649827251 scopus 로고    scopus 로고
    • Decoding the cryptic active conformation of a protein by synthetic photoscanning insulin inserts a detachable arm between receptor domains
    • Xu B, et al. (2009) Decoding the cryptic active conformation of a protein by synthetic photoscanning insulin inserts a detachable arm between receptor domains. J Biol Chem, 284:14597-14608.
    • (2009) J Biol Chem , vol.284 , pp. 14597-14608
    • Xu, B.1
  • 11
    • 33748639228 scopus 로고    scopus 로고
    • Structure of the insulin receptor ectodomain reveals a folded-over conformation
    • McKern NM, et al. (2006) Structure of the insulin receptor ectodomain reveals a folded-over conformation. Nature, 443:218-221.
    • (2006) Nature , vol.443 , pp. 218-221
    • McKern, N.M.1
  • 12
    • 4444383210 scopus 로고    scopus 로고
    • A comparison of the dynamic behavior of monomeric and dimeric insulin shows structural rearrangements in the active monomer
    • Zoete V, Meuwly M, Karplus M (2004) A comparison of the dynamic behavior of monomeric and dimeric insulin shows structural rearrangements in the active monomer. J Mol Biol, 342:913-929.
    • (2004) J Mol Biol , vol.342 , pp. 913-929
    • Zoete, V.1    Meuwly, M.2    Karplus, M.3
  • 13
    • 0029122396 scopus 로고
    • A spectroscopic investigation of the conformational dynamics of insulin in solution
    • Pittman I, Tager HS (1995) A spectroscopic investigation of the conformational dynamics of insulin in solution. Biochemistry, 34:10578-10590.
    • (1995) Biochemistry , vol.34 , pp. 10578-10590
    • Pittman, I.1    Tager, H.S.2
  • 14
    • 0031009430 scopus 로고    scopus 로고
    • Alanine scanning mutagenesis of insulin
    • Kristensen C, et al. (1997) Alanine scanning mutagenesis of insulin. J Biol Chem, 272:12978-12983.
    • (1997) J Biol Chem , vol.272 , pp. 12978-12983
    • Kristensen, C.1
  • 15
    • 0025978173 scopus 로고
    • Importance of the character and configuration of residues B24, B25, and B26 in insulin-receptor interactions
    • Mirmira RG, Nakagawa SH, Tager HS (1991) Importance of the character and configuration of residues B24, B25, and B26 in insulin-receptor interactions. J Biol Chem, 266:1428-1436.
    • (1991) J Biol Chem , vol.266 , pp. 1428-1436
    • Mirmira, R.G.1    Nakagawa, S.H.2    Tager, H.S.3
  • 16
    • 0025078913 scopus 로고
    • Monomeric insulins and their experimental and clinical implications
    • Brange J, Owens DR, Kang S, Volund A (1990) Monomeric insulins and their experimental and clinical implications. Diabetes Care, 13:923-954.
    • (1990) Diabetes Care , vol.13 , pp. 923-954
    • Brange, J.1    Owens, D.R.2    Kang, S.3    Volund, A.4
  • 17
    • 0021052991 scopus 로고
    • Studies on mutant human insulin genes: Identification and sequence analysis of a gene encoding [SerB24]insulin
    • Haneda M, Chan SJ, Kwok SC, Rubenstein AH, Steiner DF (1983) Studies on mutant human insulin genes: Identification and sequence analysis of a gene encoding [SerB24]insulin. P Natl Acad Sci USA, 80:6366-6370.
    • (1983) P Natl Acad Sci USA , vol.80 , pp. 6366-6370
    • Haneda, M.1    Chan, S.J.2    Kwok, S.C.3    Rubenstein, A.H.4    Steiner, D.F.5
  • 18
    • 0036300570 scopus 로고    scopus 로고
    • Chiral mutagenesis of insulin's hidden receptor-binding surface: Structure of an allo-isoleucine(A2) analogue
    • Xu B, et al. (2002) Chiral mutagenesis of insulin's hidden receptor-binding surface: Structure of an allo-isoleucine(A2) analogue. J Mol Biol, 316:435-441.
    • (2002) J Mol Biol , vol.316 , pp. 435-441
    • Xu, B.1
  • 19
    • 0017293453 scopus 로고
    • Receptor-binding region of insulin
    • Pullen RA, et al. (1976) Receptor-binding region of insulin. Nature, 259:369-373.
    • (1976) Nature , vol.259 , pp. 369-373
    • Pullen, R.A.1
  • 20
    • 0036782071 scopus 로고    scopus 로고
    • Structural biology of insulin and IGF1 receptors: Implications for drug design
    • De Meyts P, Whittaker J (2002) Structural biology of insulin and IGF1 receptors: Implications for drug design. Nat Rev Drug Discov, 1:769-783.
    • (2002) Nat Rev Drug Discov , vol.1 , pp. 769-783
    • De Meyts, P.1    Whittaker, J.2
  • 21
    • 34248370594 scopus 로고    scopus 로고
    • The use of Fmoc-Lys(Pac)-OH and penicillin G acylase in the preparation of novel semisynthetic insulin analogs
    • Zakova L, et al. (2007) The use of Fmoc-Lys(Pac)-OH and penicillin G acylase in the preparation of novel semisynthetic insulin analogs. J Pept Sci, 13:334-341.
    • (2007) J Pept Sci , vol.13 , pp. 334-341
    • Zakova, L.1
  • 22
    • 44349151121 scopus 로고    scopus 로고
    • Insulin analogues with modifications at position B26. Divergence of binding affinity and biological activity
    • Zakova L, et al. (2008) Insulin analogues with modifications at position B26. Divergence of binding affinity and biological activity. Biochemistry, 47:5858-5868.
    • (2008) Biochemistry , vol.47 , pp. 5858-5868
    • Zakova, L.1
  • 23
    • 0033046003 scopus 로고    scopus 로고
    • The solution structure of a superpotent B-chain-shortened single- replacement insulin analogue
    • Kurapkat G, et al. (1999) The solution structure of a superpotent B-chain-shortened single- replacement insulin analogue. Protein Sci, 8:499-508.
    • (1999) Protein Sci , vol.8 , pp. 499-508
    • Kurapkat, G.1
  • 24
    • 11144278606 scopus 로고    scopus 로고
    • Toward the insulin-IGF-I intermediate structures: Functional and structural properties of the [Tyr(B25)NMePhe(B26)] insulin mutant
    • Zakova L, et al. (2004) Toward the insulin-IGF-I intermediate structures: Functional and structural properties of the [Tyr(B25)NMePhe(B26)] insulin mutant. Biochemistry, 43:16293-16300.
    • (2004) Biochemistry , vol.43 , pp. 16293-16300
    • Zakova, L.1
  • 26
    • 0033584887 scopus 로고    scopus 로고
    • Cis peptide bonds in proteins: Residues involved, their conformations, interactions and locations
    • Pal D, Chakrabarti P (1999) Cis peptide bonds in proteins: residues involved, their conformations, interactions and locations. J Mol Biol, 294:271-288.
    • (1999) J Mol Biol , vol.294 , pp. 271-288
    • Pal, D.1    Chakrabarti, P.2
  • 27
    • 34447502323 scopus 로고    scopus 로고
    • High-performance liquid chromatography and nuclear magnetic resonance study of linear tetrapeptides and octapeptides containing N-methylated amino acid residues
    • Sykora D, Zakova L, Budesinsky M (2007) High-performance liquid chromatography and nuclear magnetic resonance study of linear tetrapeptides and octapeptides containing N-methylated amino acid residues. J Chromatogr A, 1160:128-136.
    • (2007) J Chromatogr A , vol.1160 , pp. 128-136
    • Sykora, D.1    Zakova, L.2    Budesinsky, M.3
  • 28
    • 0034419296 scopus 로고    scopus 로고
    • Chemical aspects of peptide bond isomerisation
    • Fischer G (2000) Chemical aspects of peptide bond isomerisation. Chem Soc Rev, 29:119-127.
    • (2000) Chem Soc Rev , vol.29 , pp. 119-127
    • Fischer, G.1
  • 29
    • 11944257991 scopus 로고
    • Mechanistic studies of enzymatic and nonenzymic prolyl cis-trans isomerization
    • Harrison RK, Stein RL (1992) Mechanistic studies of enzymatic and nonenzymic prolyl cis-trans isomerization. J Am Chem Soc, 114:3464-3471.
    • (1992) J Am Chem Soc , vol.114 , pp. 3464-3471
    • Harrison, R.K.1    Stein, R.L.2
  • 30
    • 65449168837 scopus 로고    scopus 로고
    • Ligand-induced activation of the insulin receptor: A multi-step process involving structural changes in both the ligand and the receptor
    • Ward CW, Lawrence MC (2009) Ligand-induced activation of the insulin receptor: A multi-step process involving structural changes in both the ligand and the receptor. Bioessays, 31:422-434.
    • (2009) Bioessays , vol.31 , pp. 422-434
    • Ward, C.W.1    Lawrence, M.C.2
  • 31
    • 0027407097 scopus 로고
    • Dynamics of a monomeric insulin analogue: Testing the molten-globule hypothesis
    • Hua QX, Ladbury JE, Weiss MA (1993) Dynamics of a monomeric insulin analogue: Testing the molten-globule hypothesis. Biochemistry, 32:1433-1442.
    • (1993) Biochemistry , vol.32 , pp. 1433-1442
    • Hua, Q.X.1    Ladbury, J.E.2    Weiss, M.A.3
  • 32
    • 0037350098 scopus 로고    scopus 로고
    • The structure of T-6 human insulin at 1.0 angstrom resolution
    • Smith GD, Pangborn WA, Blessing RH (2003) The structure of T-6 human insulin at 1.0 angstrom resolution. Acta Crystallogr D, 59:474-482.
    • (2003) Acta Crystallogr D , vol.59 , pp. 474-482
    • Smith, G.D.1    Pangborn, W.A.2    Blessing, R.H.3
  • 33
    • 0031059866 scopus 로고    scopus 로고
    • Processing of x-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W (1997) Processing of x-ray diffraction data collected in oscillation mode. Methods Enzymol, 276A:307-326.
    • (1997) Methods Enzymol , vol.276 A , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 34
    • 0028103275 scopus 로고
    • Collaborative computational project, number 4. The CCP4 suite: Programs for protein crystallography
    • Bailey S (1994) Collaborative computational project, number 4. The CCP4 suite: Programs for protein crystallography. Acta Crystallogr D, 50:760-763.
    • (1994) Acta Crystallogr D , vol.50 , pp. 760-763
    • Bailey, S.1


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