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Volumn 50, Issue 4, 2003, Pages 563-571

D-amino acid residues in peptides and proteins

Author keywords

Chirality; D configurations; Epimers; Protein Data Bank; Secondary structure; Stereoisomerism

Indexed keywords

CYCLOSPORIN; DACTINOMYCIN; DEXTRO AMINO ACID; GRAMICIDIN; POLYPEPTIDE;

EID: 0037342908     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.10320     Document Type: Article
Times cited : (51)

References (45)
  • 1
    • 0030567375 scopus 로고    scopus 로고
    • Economy in protein design: Evolution of a metal-independent beta-beta-alpha motif based on the zinc finger domains
    • Struthers MD, Cheng RP, Imperiali B. Economy in protein design: Evolution of a metal-independent beta-beta-alpha motif based on the zinc finger domains. J Am Chem Soc 1996;118:3073-3081.
    • (1996) J Am Chem Soc , vol.118 , pp. 3073-3081
    • Struthers, M.D.1    Cheng, R.P.2    Imperiali, B.3
  • 2
    • 0001511875 scopus 로고
    • A conformational study of peptides with the general structure Ac-L-Xaa-Pro-D-XaaL-Xaa-NH2: Spectroscopic evidence for a peptide with significant beta-turn character in water and dimethyl sulfoxide
    • Imperiali B, Fisher SL, Moats RA, Prins TJ. A conformational study of peptides with the general structure Ac-L-Xaa-Pro-D-XaaL-Xaa-NH2: Spectroscopic evidence for a peptide with significant beta-turn character in water and dimethyl sulfoxide. J Am Chem Soc 1992;114:3182-3188.
    • (1992) J Am Chem Soc , vol.114 , pp. 3182-3188
    • Imperiali, B.1    Fisher, S.L.2    Moats, R.A.3    Prins, T.J.4
  • 3
    • 0344835021 scopus 로고
    • Structure of cyclo-[L-threonyl-D-valyl-L-prolyl-sarcosyl-N-methyl-L-valyl-O(Thr)] at 153-K
    • Pohl E, Sheldrick GM, Fischer S, Lackner H. Structure of cyclo-[L-threonyl-D-valyl-L-prolyl-sarcosyl-N-methyl-L-valyl-O(Thr)] at 153-K. Acta Crystallogr 1994;C50:100-103.
    • (1994) Acta Crystallogr , vol.C50 , pp. 100-103
    • Pohl, E.1    Sheldrick, G.M.2    Fischer, S.3    Lackner, H.4
  • 4
    • 0030123876 scopus 로고    scopus 로고
    • On the electrostatic and steric similarity of lactam compounds and the natural substrate for bacterial cell-wall biosynthesis
    • Frau J, Price SL. On the electrostatic and steric similarity of lactam compounds and the natural substrate for bacterial cell-wall biosynthesis. J Comp-Aided Mol Des 1996;10:107-122.
    • (1996) J Comp-Aided Mol Des , vol.10 , pp. 107-122
    • Frau, J.1    Price, S.L.2
  • 5
    • 0028138608 scopus 로고
    • Conversion of L-amino to D-amino acids - A posttranslational reaction
    • Kreil G. Conversion of L-amino to D-amino acids - a posttranslational reaction. Science 1994;266:996-997.
    • (1994) Science , vol.266 , pp. 996-997
    • Kreil, G.1
  • 7
    • 0034529167 scopus 로고    scopus 로고
    • L to D amino acid isomerization in a peptide hormone is a late post-translational event occurring in specialized neurosecretory cells
    • Soyez D, Toullec JY, Ollivaux C, Geraud G. L to D amino acid isomerization in a peptide hormone is a late post-translational event occurring in specialized neurosecretory cells. J Biol Chem 2000;275:37870-37875.
    • (2000) J Biol Chem , vol.275 , pp. 37870-37875
    • Soyez, D.1    Toullec, J.Y.2    Ollivaux, C.3    Geraud, G.4
  • 8
    • 0031573474 scopus 로고    scopus 로고
    • Structure of the complex of leech-derived tryptase inhibitor (LDTI) with trypsin and modeling of the LDTI-tryptase system
    • Di Marco S, Priestle JP. Structure of the complex of leech-derived tryptase inhibitor (LDTI) with trypsin and modeling of the LDTI-tryptase system. Structure 1997;5:1465-1474.
    • (1997) Structure , vol.5 , pp. 1465-1474
    • Di Marco, S.1    Priestle, J.P.2
  • 10
  • 12
    • 0345266395 scopus 로고    scopus 로고
    • http://www.cmbi.kun.nl/gv/pdbreport/
  • 14
    • 0344403419 scopus 로고    scopus 로고
    • http://www.biochem.ucl.ac.uk/bsm/pdbsum/index.html
  • 16
    • 0002087304 scopus 로고
    • 3D search and research using the Cambridge Structural Database
    • Allen FH, Kennard O. 3D search and research using the Cambridge Structural Database. Chemical Design Automation News 1993;8:1, 31-37.
    • (1993) Chemical Design Automation News , vol.8 , pp. 1
    • Allen, F.H.1    Kennard, O.2
  • 17
    • 0033534374 scopus 로고    scopus 로고
    • Structural differences in D and L-monellin in the crystals of racemic mixture
    • Hung L-W, Kohmura M, Ariyoshi Y, Kim SH. Structural differences in D and L-monellin in the crystals of racemic mixture. J Mol Biol 1999;285:311-321.
    • (1999) J Mol Biol , vol.285 , pp. 311-321
    • Hung, L.-W.1    Kohmura, M.2    Ariyoshi, Y.3    Kim, S.H.4
  • 18
    • 0032127988 scopus 로고    scopus 로고
    • Structure of an enantiomeric protein, D-monellin at 1.8 angstrom resolution
    • Hung L-W, Kohmura M, Ariyoshi Y, Kim SH. Structure of an enantiomeric protein, D-monellin at 1.8 angstrom resolution. Acta Crystallogr 1998;D54:494-500.
    • (1998) Acta Crystallogr , vol.D54 , pp. 494-500
    • Hung, L.-W.1    Kohmura, M.2    Ariyoshi, Y.3    Kim, S.H.4
  • 19
    • 0029805817 scopus 로고    scopus 로고
    • Multiple solution conformations of the integrin-binding cyclic pentapeptide cyclo-[Ser-D-Leu-Asp-Val-Pro]: Analysis of the (phi,psi) space available to cyclic pentapeptides
    • Viles JH, Mitchell JBO, Gough SL, Doyle PM, Harris CJ, Sadler PJ, Thornton JM. Multiple solution conformations of the integrin-binding cyclic pentapeptide cyclo-[Ser-D-Leu-Asp-Val-Pro]: Analysis of the (phi,psi) space available to cyclic pentapeptides. Eur J Biochem 1996;242:352-362.
    • (1996) Eur J Biochem , vol.242 , pp. 352-362
    • Viles, J.H.1    Mitchell, J.B.O.2    Gough, S.L.3    Doyle, P.M.4    Harris, C.J.5    Sadler, P.J.6    Thornton, J.M.7
  • 20
    • 0344835020 scopus 로고    scopus 로고
    • http://www-mitchell.ch.cam.ac.uk/d-res.html
  • 21
    • 0030598361 scopus 로고    scopus 로고
    • Disallowed Ramachandran conformations of amino acid residues in protein structures
    • Gunasekaran K, Ramakrishnan C, Balaram P. Disallowed Ramachandran conformations of amino acid residues in protein structures. J Mol Biol 1996;264:191-198.
    • (1996) J Mol Biol , vol.264 , pp. 191-198
    • Gunasekaran, K.1    Ramakrishnan, C.2    Balaram, P.3
  • 23
    • 0030039296 scopus 로고    scopus 로고
    • PROMOTIF - A program to identify and analyze structural motifs in proteins
    • Hutchinson EG, Thornton JM. PROMOTIF - a program to identify and analyze structural motifs in proteins. Protein Sci 1996;5:212-220.
    • (1996) Protein Sci , vol.5 , pp. 212-220
    • Hutchinson, E.G.1    Thornton, J.M.2
  • 24
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W, Sander C. Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 1983;22:2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 25
    • 0028178377 scopus 로고
    • Three-dimensional structure of beta-galactosidase from E. coli
    • Jacobson RH, Zhang X-J, DuBose RF, Matthews BW. Three-dimensional structure of beta-galactosidase from E. coli. Nature 1994;369:761-766.
    • (1994) Nature , vol.369 , pp. 761-766
    • Jacobson, R.H.1    Zhang, X.-J.2    DuBose, R.F.3    Matthews, B.W.4
  • 26
    • 0031016185 scopus 로고    scopus 로고
    • Structural mapping of the catalytic mechanism for a mammalian phosphoinositide-specific phospholipase C
    • Essen LO, Perisic O, Katan M, Wu YQ, Roberts MF, Williams RL. Structural mapping of the catalytic mechanism for a mammalian phosphoinositide-specific phospholipase C. Biochemistry 1997;36:1704-1718.
    • (1997) Biochemistry , vol.36 , pp. 1704-1718
    • Essen, L.O.1    Perisic, O.2    Katan, M.3    Wu, Y.Q.4    Roberts, M.F.5    Williams, R.L.6
  • 28
    • 0028901184 scopus 로고
    • Octahedral co-ordination at the high-affinity metal site in enolase: Crystallographic analysis of the Mg(II)-enzyme complex from yeast at 1.9 Å resolution
    • Wedekind JE, Reed GH, Rayment I. Octahedral co-ordination at the high-affinity metal site in enolase: Crystallographic analysis of the Mg(II)-enzyme complex from yeast at 1.9 Å resolution, Biochemistry 1995;34:4325-4330.
    • (1995) Biochemistry , vol.34 , pp. 4325-4330
    • Wedekind, J.E.1    Reed, G.H.2    Rayment, I.3
  • 32
    • 0025923565 scopus 로고
    • 1.9-Å structures of ternary complexes of citrate synthase with D- and L-malate: Mechanistic implications
    • Karpusas M, Holland D, Remington SJ. 1.9-Å structures of ternary complexes of citrate synthase with D- and L-malate: Mechanistic implications. Biochemistry 1991;30:6024-6031.
    • (1991) Biochemistry , vol.30 , pp. 6024-6031
    • Karpusas, M.1    Holland, D.2    Remington, S.J.3
  • 33
    • 0021590971 scopus 로고
    • Crystal structure analysis and molecular model of a complex of citrate synthase with oxaloactate and s-acetonyl coenzyme A
    • Wiegand G, Remington SJ, Deisenhofer J, Huber R. Crystal structure analysis and molecular model of a complex of citrate synthase with oxaloactate and s-acetonyl coenzyme A. J Mol Biol 1984;174:205-219.
    • (1984) J Mol Biol , vol.174 , pp. 205-219
    • Wiegand, G.1    Remington, S.J.2    Deisenhofer, J.3    Huber, R.4
  • 35
    • 0030593029 scopus 로고    scopus 로고
    • Design of a monomeric 23-residue polypeptide with defined tertiary structure
    • Struthers MD, Cheng RP, Imperiali B. Design of a monomeric 23-residue polypeptide with defined tertiary structure. Science 1996;271:342-345.
    • (1996) Science , vol.271 , pp. 342-345
    • Struthers, M.D.1    Cheng, R.P.2    Imperiali, B.3
  • 36
    • 0034995131 scopus 로고    scopus 로고
    • Design of a discretely folded mini-protein motif with predominantly beta-structure
    • Ottesen JJ, Imperiali B. Design of a discretely folded mini-protein motif with predominantly beta-structure. Nat Struct Biol 2001;8:535-539.
    • (2001) Nat Struct Biol , vol.8 , pp. 535-539
    • Ottesen, J.J.1    Imperiali, B.2
  • 37
    • 0031928726 scopus 로고    scopus 로고
    • Design strategies for the construction of independently folded polypeptide motifs
    • Imperiali B, Ottesen JJ. Design strategies for the construction of independently folded polypeptide motifs. Biopolymers 1998;47:23-29.
    • (1998) Biopolymers , vol.47 , pp. 23-29
    • Imperiali, B.1    Ottesen, J.J.2
  • 39
    • 18244430466 scopus 로고    scopus 로고
    • Non-centrosymmetric racemates: Space-group frequencies and conformational similarities between crystallographically independent molecules
    • Dalhus B, Görbitz CH. Non-centrosymmetric racemates: Space-group frequencies and conformational similarities between crystallographically independent molecules. Acta Crystallogr 2000;B56:715-719.
    • (2000) Acta Crystallogr , vol.B56 , pp. 715-719
    • Dalhus, B.1    Görbitz, C.H.2
  • 40
    • 0025890946 scopus 로고
    • Influence of proline residues on protein conformation
    • MacArthur MW, Thornton JM. Influence of proline residues on protein conformation. J Mol Biol 1991;218:397-412.
    • (1991) J Mol Biol , vol.218 , pp. 397-412
    • MacArthur, M.W.1    Thornton, J.M.2
  • 41
    • 0020479083 scopus 로고
    • The structure of melittin: I. Structure determination and partial refinement
    • Terwilliger TC, Eisenberg D. The structure of melittin: I. Structure determination and partial refinement. J Biol Chem 1982;257:6010-6015.
    • (1982) J Biol Chem , vol.257 , pp. 6010-6015
    • Terwilliger, T.C.1    Eisenberg, D.2
  • 42
    • 0034709431 scopus 로고    scopus 로고
    • The helix-destabilizing propensity scale of D-amino acids: The influence of side chain steric effects
    • Krause E, Bienert M, Schmieder P, Wenschuh H. The helix-destabilizing propensity scale of D-amino acids: The influence of side chain steric effects. J Am Chem Soc 2000;122:4865-4870.
    • (2000) J Am Chem Soc , vol.122 , pp. 4865-4870
    • Krause, E.1    Bienert, M.2    Schmieder, P.3    Wenschuh, H.4
  • 43
    • 0036185353 scopus 로고    scopus 로고
    • Determination of stereochemistry stability coefficients of amino acid side-chains in an amphipathic α-helix
    • Chen Y, Mant CT, Hodges RS. Determination of stereochemistry stability coefficients of amino acid side-chains in an amphipathic α-helix. J Peptide Res 2002;59:18-33.
    • (2002) J Peptide Res , vol.59 , pp. 18-33
    • Chen, Y.1    Mant, C.T.2    Hodges, R.S.3
  • 44
    • 0026750901 scopus 로고
    • The helix-forming propensity of D-alanine in a right-handed alpha-helix
    • Fairman R, Anthony-Cahill SJ, Degrado WF. The helix-forming propensity of D-alanine in a right-handed alpha-helix. J Am Chem Soc 1992;114:5458-5459.
    • (1992) J Am Chem Soc , vol.114 , pp. 5458-5459
    • Fairman, R.1    Anthony-Cahill, S.J.2    Degrado, W.F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.