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Volumn 278, Issue 1, 1998, Pages 231-238

Succinimide and isoaspartate residues in the crystal structures of hen egg-white lysozyme complexed with tri-N-acetylchitotriose

Author keywords

Crystal structure; Hen egg white lysozyme; Isoaspartate; Post translational modification; Succinimide

Indexed keywords

ASPARTIC ACID; EGG WHITE; LIGAND; LYSOZYME; SUCCINIMIDE; TRI N ACETYLCHITOTRIOSE; TRIOSE; UNCLASSIFIED DRUG;

EID: 0032562736     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.1674     Document Type: Article
Times cited : (43)

References (37)
  • 4
    • 0027971497 scopus 로고
    • Three-dimensional structures of the free and the antigen-complexed Fab form monoclonal anti-lysozyme antibody D44.1
    • Braden B.C., Souchon H., Eisele J.-L., Bentley G.A., Bhat T.N., Navaza J., Poljak R.J. Three-dimensional structures of the free and the antigen-complexed Fab form monoclonal anti-lysozyme antibody D44.1. J. Mol. Biol. 243:1994;767-781
    • (1994) J. Mol. Biol. , vol.243 , pp. 767-781
    • Braden, B.C.1    Souchon, H.2    Eisele, J.-L.3    Bentley, G.A.4    Bhat, T.N.5    Navaza, J.6    Poljak, R.J.7
  • 5
    • 0029075220 scopus 로고
    • Effect of adjacent histidine and cysteine residues on the spontaneous degradation of asparaginyl- and aspartyl-containing peptides
    • 547-533
    • Brennan T.V., Clarke S. Effect of adjacent histidine and cysteine residues on the spontaneous degradation of asparaginyl- and aspartyl-containing peptides. Int. J. Pept. Protein Res. 45:1995;. 547-533
    • (1995) Int. J. Pept. Protein Res. , vol.45
    • Brennan, T.V.1    Clarke, S.2
  • 6
    • 0027992730 scopus 로고
    • Repair of spontaneously deamidated HPr phosphocarrier protein catalyzed by the L -isoaspartate-(D -aspartate) O -Methyltransferase
    • Brennan T.V., Anderson J.W., Jia Z., Waygood E.B., Clarke S. Repair of spontaneously deamidated HPr phosphocarrier protein catalyzed by the L -isoaspartate-(D -aspartate) O -Methyltransferase. J. Biol. Chem. 269:1994;24586-24595
    • (1994) J. Biol. Chem. , vol.269 , pp. 24586-24595
    • Brennan, T.V.1    Anderson, J.W.2    Jia, Z.3    Waygood, E.B.4    Clarke, S.5
  • 8
    • 0030022071 scopus 로고    scopus 로고
    • Isomerization of an aspartic acid residue in the complementarity-determining regions of a recombinant antibody to human IgE: Identification and effect on binding affinity
    • Cacia J., Keck R., Presta L.G., Frenz J. Isomerization of an aspartic acid residue in the complementarity-determining regions of a recombinant antibody to human IgE identification and effect on binding affinity. Biochemistry. 35:1996;1897-1903
    • (1996) Biochemistry , vol.35 , pp. 1897-1903
    • Cacia, J.1    Keck, R.2    Presta, L.G.3    Frenz, J.4
  • 9
    • 0024487067 scopus 로고
    • Solid-state conformations of aminosuccinyl peptides: Crystal structure of tert -Butyloxycarbonyl- L -leucyl- L -aminosuccinyl- L -phenylalaninamide
    • Capasso S., Mazzarella L., Sica F., Zagari A. Solid-state conformations of aminosuccinyl peptides crystal structure of tert -Butyloxycarbonyl- L -leucyl- L -aminosuccinyl- L -phenylalaninamide. Biopolymers. 28:1989;139-147
    • (1989) Biopolymers , vol.28 , pp. 139-147
    • Capasso, S.1    Mazzarella, L.2    Sica, F.3    Zagari, A.4
  • 10
    • 24444452411 scopus 로고
    • Solid-state conformations of aminosuccinyl peptides: Structure of tert -butyloxycarbonyl- L -prolyl- L -aminosuccinyl-glycyl- L -alanine methyl ester (Boc- L -Pro- L -Asu-Gly- L -Ala-OMe). a case of pseudo-translational symmetry
    • Capasso S., Mazzarella L., Sica F., Zagari A. Solid-state conformations of aminosuccinyl peptides structure of tert -butyloxycarbonyl- L -prolyl- L -aminosuccinyl-glycyl- L -alanine methyl ester (Boc- L -Pro- L -Asu-Gly- L -Ala-OMe). A case of pseudo-translational symmetry. Acta Crystallog. sect. B. 48:1992;285-290
    • (1992) Acta Crystallog. Sect. B , vol.48 , pp. 285-290
    • Capasso, S.1    Mazzarella, L.2    Sica, F.3    Zagari, A.4
  • 11
  • 12
    • 0030040277 scopus 로고    scopus 로고
    • Interactions of protein antigens with antibodies
    • Davies D.R., Cohen G.H. Interactions of protein antigens with antibodies. Proc. Natl Acad. Sci. USA. 93:1996;7-12
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 7-12
    • Davies, D.R.1    Cohen, G.H.2
  • 14
    • 0028065058 scopus 로고
    • Simultaneous stereoinversion and isomerization at specific aspartic acid residues in αa-crystallin from human lens
    • Fujii N., Satoh K., Harada K., Ishibashi Y. Simultaneous stereoinversion and isomerization at specific aspartic acid residues in αA-crystallin from human lens. J. Biochem. 116:1994;663-669
    • (1994) J. Biochem , vol.116 , pp. 663-669
    • Fujii, N.1    Satoh, K.2    Harada, K.3    Ishibashi, Y.4
  • 15
    • 0028218937 scopus 로고
    • Simultaneous racemization and isomerization at specific aspartic acid residues in αb-crystallin from the aged human lens
    • Fujii N., Ishibashi Y., Satoh K., Fujino M., Harada K. Simultaneous racemization and isomerization at specific aspartic acid residues in αB-crystallin from the aged human lens. Biochim. Biophys. Acta. 1204:1994;157-163
    • (1994) Biochim. Biophys. Acta , vol.1204 , pp. 157-163
    • Fujii, N.1    Ishibashi, Y.2    Satoh, K.3    Fujino, M.4    Harada, K.5
  • 16
    • 0023109951 scopus 로고
    • Deamidation, isomerization, and racemization at asparaginyl and aspartyl residues in peptides: Succinimide-linked reactions that contribute to protein degradation
    • Geiger T., Clarke S. Deamidation, isomerization, and racemization at asparaginyl and aspartyl residues in peptides Succinimide-linked reactions that contribute to protein degradation. J. Biol. Chem. 262:1987;785-794
    • (1987) J. Biol. Chem. , vol.262 , pp. 785-794
    • Geiger, T.1    Clarke, S.2
  • 17
    • 0023433637 scopus 로고
    • Crystal and molecular structures of the isomeric dipeptides α- L -aspartyl- L -alanine and β- L -aspartyl- L -alanine
    • Görbitz C.H. Crystal and molecular structures of the isomeric dipeptides α- L -aspartyl- L -alanine and β- L -aspartyl- L -alanine. Acta Chem. Scand. B 41:1987;679-685
    • (1987) Acta Chem. Scand. , vol.41 , pp. 679-685
    • Görbitz, C.H.1
  • 18
    • 0028172551 scopus 로고
    • Protein hydration observed by X-ray diffraction
    • Jiang J.-S., Brünger A.T. Protein hydration observed by X-ray diffraction. J. Mol. Biol. 243:1994;100-115
    • (1994) J. Mol. Biol. , vol.243 , pp. 100-115
    • Jiang, J.-S.1    Brünger, A.T.2
  • 20
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P.J. MOLSCRIPT A program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24:1991;946-950
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 21
    • 0029140564 scopus 로고
    • The influence of temperature on lysozyme crystals. Structure and dynamics of protein and water
    • Kurinov I.V., Harrison R.W. The influence of temperature on lysozyme crystals. Structure and dynamics of protein and water. Acta Crystallog. sect. D. 51:1995;98-109
    • (1995) Acta Crystallog. Sect. D , vol.51 , pp. 98-109
    • Kurinov, I.V.1    Harrison, R.W.2
  • 22
    • 0001099937 scopus 로고
    • Traitement statistique des erreurs dans la determination des structures cristallines
    • Luzzati V. Traitement statistique des erreurs dans la determination des structures cristallines. Acta Crystallog. 5:1952;802-810
    • (1952) Acta Crystallog. , vol.5 , pp. 802-810
    • Luzzati, V.1
  • 23
    • 0028934071 scopus 로고
    • Dissection of protein-carbohydrate interactions in mutant hen egg-white lysozyme complexes and their hydrolytic activity
    • Maenaka K., Matsushima M., Song H., Sunada F., Watanabe K., Kumagai I. Dissection of protein-carbohydrate interactions in mutant hen egg-white lysozyme complexes and their hydrolytic activity. J. Mol. Biol. 247:1995;281-293
    • (1995) J. Mol. Biol. , vol.247 , pp. 281-293
    • Maenaka, K.1    Matsushima, M.2    Song, H.3    Sunada, F.4    Watanabe, K.5    Kumagai, I.6
  • 24
    • 0030566050 scopus 로고    scopus 로고
    • Crystallography of succinimide hen egg-white lysozyme at low temperatures
    • Miyawaki K., Noguchi S., Harada S., Satow Y. Crystallography of succinimide hen egg-white lysozyme at low temperatures. J. Cryst. Growth. 168:1996;292-296
    • (1996) J. Cryst. Growth , vol.168 , pp. 292-296
    • Miyawaki, K.1    Noguchi, S.2    Harada, S.3    Satow, Y.4
  • 25
    • 0029876218 scopus 로고    scopus 로고
    • Molecular aging of tubulin: Accumulation of isoaspartyl sites in vitro and in vivo
    • Najbauer J., Orpiszewski J., Aswad D.W. Molecular aging of tubulin Accumulation of isoaspartyl sites in vitro and in vivo. Biochemistry. 35:1996;5183-5190
    • (1996) Biochemistry , vol.35 , pp. 5183-5190
    • Najbauer, J.1    Orpiszewski, J.2    Aswad, D.W.3
  • 27
    • 0028260569 scopus 로고
    • Chemical pathways of peptide degradation. VI. Effect of the primary sequence on the pathways of degradation of aspartyl residues in model hexapeptides
    • Oliyai C., Borchardt R.T. Chemical pathways of peptide degradation. VI. Effect of the primary sequence on the pathways of degradation of aspartyl residues in model hexapeptides. Pharm. Res. 11:1994;751-758
    • (1994) Pharm. Res. , vol.11 , pp. 751-758
    • Oliyai, C.1    Borchardt, R.T.2
  • 28
    • 0002452464 scopus 로고
    • Oscillation data reduction program
    • Warrington, U.K: SERC Daresbury Laboratory
    • Otwinowski Z. Oscillation data reduction program. Proceedings of the CCP4 Study Weekend. 1993;56-62 SERC Daresbury Laboratory, Warrington, U.K
    • (1993) Proceedings of the CCP4 Study Weekend , pp. 56-62
    • Otwinowski, Z.1
  • 29
    • 0029112135 scopus 로고
    • Spontaneous alterations in the covalent structure of synapsin I during in vitro aging
    • Paranandi M.V., Aswad D.W. Spontaneous alterations in the covalent structure of synapsin I during in vitro aging. Biochem. Biophys. Res. Commun. 212:1995;442-448
    • (1995) Biochem. Biophys. Res. Commun. , vol.212 , pp. 442-448
    • Paranandi, M.V.1    Aswad, D.W.2
  • 32
    • 0031105467 scopus 로고    scopus 로고
    • Protein splicing: Occurrence, mechanisms and related phenomena
    • Shao Y., Kent S.B.H. Protein splicing occurrence, mechanisms and related phenomena. Chem. Biol. 4:1997;187-194
    • (1997) Chem. Biol. , vol.4 , pp. 187-194
    • Shao, Y.1    Kent, S.B.H.2
  • 33
    • 0029124041 scopus 로고
    • Protein splicing: Characterization of the aminosuccinimide residues at the carboxyl terminus of the excised intervening sequence
    • Shao Y., Xu M.Q., Paulus H. Protein splicing Characterization of the aminosuccinimide residues at the carboxyl terminus of the excised intervening sequence. Biochemistry. 34:1995;10844-10850
    • (1995) Biochemistry , vol.34 , pp. 10844-10850
    • Shao, Y.1    Xu, M.Q.2    Paulus, H.3
  • 34
    • 0028905409 scopus 로고
    • Protein L -isoaspartyl methyltransferase: Developmentally regulated gene expression and protein localization in the central nervous system of aged rat
    • Shirasawa T., Endoh R., Zeng Y.X., Sakamoto K., Mori H. Protein L -isoaspartyl methyltransferase Developmentally regulated gene expression and protein localization in the central nervous system of aged rat. Neurosci. Letters. 188:1995;37-40
    • (1995) Neurosci. Letters , vol.188 , pp. 37-40
    • Shirasawa, T.1    Endoh, R.2    Zeng, Y.X.3    Sakamoto, K.4    Mori, H.5
  • 35
    • 0028030490 scopus 로고
    • Isolation and characterization of 101-succinimide lysozyme that possesses the cyclic imide at Asp101-Gly 102
    • Tomizawa H., Yamada H., Ueda T., Imoto T. Isolation and characterization of 101-succinimide lysozyme that possesses the cyclic imide at Asp101-Gly 102. Biochemistry. 33:1994;8770-8774
    • (1994) Biochemistry , vol.33 , pp. 8770-8774
    • Tomizawa, H.1    Yamada, H.2    Ueda, T.3    Imoto, T.4
  • 36
    • 0000695363 scopus 로고    scopus 로고
    • High-resolution structure (1.33 Å) of a HEW lysozyme tetragonal crystal grown in the APCF apparatus. Data and structural comparison with a crystal grown under microgravity from SpaceHab-01 mission
    • Vaney M.C., Maignan S., Riès-Kautt M., Ducruix A. High-resolution structure (1.33 Å) of a HEW lysozyme tetragonal crystal grown in the APCF apparatus. Data and structural comparison with a crystal grown under microgravity from SpaceHab-01 mission. Acta Crystallog. sect. D. 52:1996;505-517
    • (1996) Acta Crystallog. Sect. D , vol.52 , pp. 505-517
    • Vaney, M.C.1    Maignan, S.2    Riès-Kautt, M.3    Ducruix, A.4
  • 37
    • 0014347799 scopus 로고
    • Stereochemical criteria for polypeptides and proteins. V. Conformation of a system of three linked peptide units
    • Venkatachalam C.M. Stereochemical criteria for polypeptides and proteins. V. Conformation of a system of three linked peptide units. Biopolymers. 6:1968;1425-1436
    • (1968) Biopolymers , vol.6 , pp. 1425-1436
    • Venkatachalam, C.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.