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Volumn 1649, Issue 1, 2003, Pages 85-96

Aromatic side-chain interactions in proteins. Near- and far-sequence His-X pairs

Author keywords

Aromatic amino acid; Aromatic interaction; Aromatic pair; Heteroatom interaction; Histidine; Secondary structures

Indexed keywords

HISTIDINE; PHENYLALANINE; TRYPTOPHAN; TYROSINE; AROMATIC AMINO ACID; PROTEIN;

EID: 0043123270     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1570-9639(03)00161-4     Document Type: Article
Times cited : (43)

References (41)
  • 1
    • 0242407760 scopus 로고    scopus 로고
    • An essential role of Glu-243 and His-239 in the phosphotransfer reaction catalyzed by pyruvate dehydrogenase kinase
    • Tuganova A., Yoder M.D., Popov K.M. An essential role of Glu-243 and His-239 in the phosphotransfer reaction catalyzed by pyruvate dehydrogenase kinase. J. Biol. Chem. 276:2001;17994-17999.
    • (2001) J. Biol. Chem. , vol.276 , pp. 17994-17999
    • Tuganova, A.1    Yoder, M.D.2    Popov, K.M.3
  • 2
    • 0035048410 scopus 로고    scopus 로고
    • His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition state
    • Huber R.E., Hlede I.Y., Roth N.J., McKenzie K.C., Ghumman K.K. His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition state. Biochem. Cell. Biol. 79:2001;183-193.
    • (2001) Biochem. Cell. Biol. , vol.79 , pp. 183-193
    • Huber, R.E.1    Hlede, I.Y.2    Roth, N.J.3    McKenzie, K.C.4    Ghumman, K.K.5
  • 3
    • 0035826676 scopus 로고    scopus 로고
    • Involvement of the Arg-Asp-His catalytic triad in enzymatic cleavage of the phosphodiester bond
    • Kubiak R.J., Yue X., Hondal R.J., Mihai C., Tsai M.D., Bruzik K.S. Involvement of the Arg-Asp-His catalytic triad in enzymatic cleavage of the phosphodiester bond. Biochemistry. 40:2001;5422-5432.
    • (2001) Biochemistry , vol.40 , pp. 5422-5432
    • Kubiak, R.J.1    Yue, X.2    Hondal, R.J.3    Mihai, C.4    Tsai, M.D.5    Bruzik, K.S.6
  • 4
    • 0035964293 scopus 로고    scopus 로고
    • On the multiple functional roles of the active site histidine in catalysis and allosteric regulation of Escherichia coli glucosamine 6-phosphate deaminase
    • Montero-Moran G.M., Lara-Gonzalez S., Alvarez-Anorve L.I., Plumbridge J.A., Calcagno M.L. On the multiple functional roles of the active site histidine in catalysis and allosteric regulation of Escherichia coli glucosamine 6-phosphate deaminase. Biochemistry. 40:2001;10187-10196.
    • (2001) Biochemistry , vol.40 , pp. 10187-10196
    • Montero-Moran, G.M.1    Lara-Gonzalez, S.2    Alvarez-Anorve, L.I.3    Plumbridge, J.A.4    Calcagno, M.L.5
  • 6
    • 0032890433 scopus 로고    scopus 로고
    • Receptor recognition by histidine 16 of human epidermal growth factor via hydrogen-bond donor/acceptor interactions
    • Nandagopal K., Terzaghi-Howe M., Niyogi S.K. Receptor recognition by histidine 16 of human epidermal growth factor via hydrogen-bond donor/acceptor interactions. J. Cell. Biochem. 72:1999;16-24.
    • (1999) J. Cell. Biochem. , vol.72 , pp. 16-24
    • Nandagopal, K.1    Terzaghi-Howe, M.2    Niyogi, S.K.3
  • 7
    • 0020119906 scopus 로고
    • A salt bridge stabilizes the helix formed by isolated C-peptide of RNase a
    • Bierzynski A., Kim P.S., Baldwin R.L. A salt bridge stabilizes the helix formed by isolated C-peptide of RNase A. Proc. Natl. Acad. Sci. U. S. A. 79:1982;2470-2474.
    • (1982) Proc. Natl. Acad. Sci. U. S. A. , vol.79 , pp. 2470-2474
    • Bierzynski, A.1    Kim, P.S.2    Baldwin, R.L.3
  • 8
    • 0033200372 scopus 로고    scopus 로고
    • Secondary ligands enhance affinity at a designed metal-binding site
    • Marino S.F., Regan L. Secondary ligands enhance affinity at a designed metal-binding site. Chem. Biol. 6:1999;649-655.
    • (1999) Chem. Biol. , vol.6 , pp. 649-655
    • Marino, S.F.1    Regan, L.2
  • 9
    • 0019334147 scopus 로고
    • Neutron diffraction identifies His 57 as the catalytic base in trypsin
    • Kossiakoff A.A., Spencer S.A. Neutron diffraction identifies His 57 as the catalytic base in trypsin. Nature. 288:1980;414-416.
    • (1980) Nature , vol.288 , pp. 414-416
    • Kossiakoff, A.A.1    Spencer, S.A.2
  • 10
    • 0019889789 scopus 로고
    • Direct determination of the protonation states of aspartic acid-102 and histidine-57 in the tetrahedral intermediate of the serine proteases: Neutron structure of trypsin
    • Kossiakoff A.A., Spencer S.A. Direct determination of the protonation states of aspartic acid-102 and histidine-57 in the tetrahedral intermediate of the serine proteases: neutron structure of trypsin. Biochemistry. 20:1981;6462-6474.
    • (1981) Biochemistry , vol.20 , pp. 6462-6474
    • Kossiakoff, A.A.1    Spencer, S.A.2
  • 11
    • 0033106249 scopus 로고    scopus 로고
    • Exploring protein interiors: The role of a buried histidine in the KH module fold
    • Fraternali F., Amodeo P., Musco G., Nilges M., Pastore A. Exploring protein interiors: the role of a buried histidine in the KH module fold. Proteins. 34:1999;484-496.
    • (1999) Proteins , vol.34 , pp. 484-496
    • Fraternali, F.1    Amodeo, P.2    Musco, G.3    Nilges, M.4    Pastore, A.5
  • 12
    • 0026525805 scopus 로고
    • Histidine-aromatic interactions in Barnase. Elevation of Histidine pKa and contribution to protein stability
    • Loewenthal R., Sancho J., Fersht A.R. Histidine-aromatic interactions in Barnase. Elevation of Histidine pKa and contribution to protein stability. J. Mol. Biol. 224:1992;759-770.
    • (1992) J. Mol. Biol. , vol.224 , pp. 759-770
    • Loewenthal, R.1    Sancho, J.2    Fersht, A.R.3
  • 13
    • 0029930588 scopus 로고    scopus 로고
    • Contribution to activity of Histidine-aromatic, amide-aromatic, and aromatic-aromatic interactions in the extended catalytic site of Cysteine proteinases
    • Bromme D., Bonneau P.R., Purisima E., Lachance P., Hajnik S., Thomas D.Y., Storer A.C. Contribution to activity of Histidine-aromatic, amide-aromatic, and aromatic-aromatic interactions in the extended catalytic site of Cysteine proteinases. Biochemistry. 35:1996;3970-3979.
    • (1996) Biochemistry , vol.35 , pp. 3970-3979
    • Bromme, D.1    Bonneau, P.R.2    Purisima, E.3    Lachance, P.4    Hajnik, S.5    Thomas, D.Y.6    Storer, A.C.7
  • 15
    • 0027398886 scopus 로고
    • The (I,I+4) Phe-His interaction studied in an alanine-based α-helix
    • Armstrong K.M., Fairman R., Baldwin R.L. The (I,I+4) Phe-His interaction studied in an alanine-based α-helix. J. Mol. Biol. 230:1993;284-291.
    • (1993) J. Mol. Biol. , vol.230 , pp. 284-291
    • Armstrong, K.M.1    Fairman, R.2    Baldwin, R.L.3
  • 16
    • 0030991899 scopus 로고    scopus 로고
    • Roles of histidine 31 and tryptophan 34 in the structure, self-association, and folding of murine interleukin-6
    • Matthews J.M., Ward L.D., Hammacher A., Norton R.S., Simpson R.J. Roles of histidine 31 and tryptophan 34 in the structure, self-association, and folding of murine interleukin-6. Biochemistry. 36:1997;6187-6196.
    • (1997) Biochemistry , vol.36 , pp. 6187-6196
    • Matthews, J.M.1    Ward, L.D.2    Hammacher, A.3    Norton, R.S.4    Simpson, R.J.5
  • 17
    • 0027400789 scopus 로고
    • Aromatic-histidine interactions in the zinc finger motif: Structural inequivalence of Phenylalanine and Tyrosine in the hydrophobic core
    • Jasanoff A., Weiss M.A. Aromatic-histidine interactions in the zinc finger motif: structural inequivalence of Phenylalanine and Tyrosine in the hydrophobic core. Biochemistry. 32:1993;1423-1432.
    • (1993) Biochemistry , vol.32 , pp. 1423-1432
    • Jasanoff, A.1    Weiss, M.A.2
  • 18
    • 0033597235 scopus 로고    scopus 로고
    • The structure and unusual pH dependence of plastocyanin from the fern Dryopteris crassirhizoma. The protonation of an active site histidine is hindered by pi-pi interactions
    • Kohzuma T., Inoue T., Yoshizaki F., Sasakawa Y., Onodera K., Nagatomo S., Kitagawa T., Uzawa S., Isobe Y., Sugimura Y., Gotowda M., Kai Y. The structure and unusual pH dependence of plastocyanin from the fern Dryopteris crassirhizoma. The protonation of an active site histidine is hindered by pi-pi interactions. J. Biol. Chem. 274:1999;11817-11823.
    • (1999) J. Biol. Chem. , vol.274 , pp. 11817-11823
    • Kohzuma, T.1    Inoue, T.2    Yoshizaki, F.3    Sasakawa, Y.4    Onodera, K.5    Nagatomo, S.6    Kitagawa, T.7    Uzawa, S.8    Isobe, Y.9    Sugimura, Y.10    Gotowda, M.11    Kai, Y.12
  • 19
    • 0032054015 scopus 로고    scopus 로고
    • CH/π interactions as demonstrated in the crystal structure of guanine-nucleotide binding proteins, src homology-2 domains and human growth hormone in complex with their specific ligands
    • Umezama Y., Nishio M. CH/π interactions as demonstrated in the crystal structure of guanine-nucleotide binding proteins, src homology-2 domains and human growth hormone in complex with their specific ligands. Bioorg. Med. Chem. 6:1998;493-504.
    • (1998) Bioorg. Med. Chem. , vol.6 , pp. 493-504
    • Umezama, Y.1    Nishio, M.2
  • 20
    • 0033798257 scopus 로고    scopus 로고
    • CH/π interactions in the crystal structure of TATA-box binding protein/DNA complexes
    • Umezama Y., Nishio M. CH/π interactions in the crystal structure of TATA-box binding protein/DNA complexes. Bioorg. Med. Chem. 8:2000;2643-2650.
    • (2000) Bioorg. Med. Chem. , vol.8 , pp. 2643-2650
    • Umezama, Y.1    Nishio, M.2
  • 21
    • 0003505803 scopus 로고    scopus 로고
    • The CH/π interaction. Evidence, nature, and consequences, in series
    • A.P. Marchand. New York: Wiley-VCH
    • Nishio M., Hirota M., Umezawa Y. The CH/π interaction. Evidence, nature, and consequences, in series. Marchand A.P. Methods in Stereochemical Analysis. 1998;Wiley-VCH, New York.
    • (1998) Methods in Stereochemical Analysis
    • Nishio, M.1    Hirota, M.2    Umezawa, Y.3
  • 23
    • 0022419375 scopus 로고
    • Aromatic-aromatic interaction: A mechanism of protein structure stabilization
    • Burley S.K., Petsko G.A. Aromatic-aromatic interaction: a mechanism of protein structure stabilization. Science. 229:1985;23-28.
    • (1985) Science , vol.229 , pp. 23-28
    • Burley, S.K.1    Petsko, G.A.2
  • 24
    • 0027209738 scopus 로고
    • Hydrophobic core repacking and aromatic-aromatic interaction in the thermostable mutant of T4 lysozyme Ser 117→Phe
    • Anderson D.E., Hurley J.H., Nicholson H., Haase W.A., Matthews B.W. Hydrophobic core repacking and aromatic-aromatic interaction in the thermostable mutant of T4 lysozyme Ser 117→Phe. Protein Sci. 2:1993;1285-1290.
    • (1993) Protein Sci. , vol.2 , pp. 1285-1290
    • Anderson, D.E.1    Hurley, J.H.2    Nicholson, H.3    Haase, W.A.4    Matthews, B.W.5
  • 25
    • 0025756736 scopus 로고
    • Aromatic-aromatic interactions and protein stability. Investigation by double mutant cycle
    • Serrano L., Bycroft M., Fersht A.R. Aromatic-aromatic interactions and protein stability. Investigation by double mutant cycle. J. Mol. Biol. 218:1991;465-475.
    • (1991) J. Mol. Biol. , vol.218 , pp. 465-475
    • Serrano, L.1    Bycroft, M.2    Fersht, A.R.3
  • 26
    • 0036643478 scopus 로고    scopus 로고
    • The nature of intermolecular interactions between aromatic amino acid residues
    • Gervasio F.L., Chelli R., Procacci P., Schettino V. The nature of intermolecular interactions between aromatic amino acid residues. Proteins. 48:2002;117-125.
    • (2002) Proteins , vol.48 , pp. 117-125
    • Gervasio, F.L.1    Chelli, R.2    Procacci, P.3    Schettino, V.4
  • 27
    • 0343293808 scopus 로고    scopus 로고
    • An additional aromatic interaction improves the thermostability and thermophilicity of a mesophilic family 11 xylanase: Structural basis and molecular study
    • Georis J., de Lemos Esteves F., Lamotte-Brasseur J., Bougnet V., Devreese B., Giannotta F., Granier B., Frere J.M. An additional aromatic interaction improves the thermostability and thermophilicity of a mesophilic family 11 xylanase: structural basis and molecular study. Protein Sci. 9:2000;466-475.
    • (2000) Protein Sci. , vol.9 , pp. 466-475
    • Georis, J.1    De Lemos Esteves, F.2    Lamotte-Brasseur, J.3    Bougnet, V.4    Devreese, B.5    Giannotta, F.6    Granier, B.7    Frere, J.M.8
  • 28
    • 0034495733 scopus 로고    scopus 로고
    • Aromatic clusters: A determinant of thermal stability of thermophilic proteins
    • Kannan N., Vishveshwara S. Aromatic clusters: a determinant of thermal stability of thermophilic proteins. Protein Eng. 13:2000;753-761.
    • (2000) Protein Eng. , vol.13 , pp. 753-761
    • Kannan, N.1    Vishveshwara, S.2
  • 29
    • 0037487158 scopus 로고    scopus 로고
    • Significance of aromatic-backbone amide interactions in protein structure
    • Tóth G., Watts C.R., Murphy R.F., Lovas S. Significance of aromatic-backbone amide interactions in protein structure. Proteins. 43:2001;373-381.
    • (2001) Proteins , vol.43 , pp. 373-381
    • Tóth, G.1    Watts, C.R.2    Murphy, R.F.3    Lovas, S.4
  • 30
    • 0342810084 scopus 로고
    • The interaction between phenylalanine rings in proteins
    • Singh J., Thornton J.M. The interaction between phenylalanine rings in proteins. FEBS Lett. 191:1985;1-6.
    • (1985) FEBS Lett. , vol.191 , pp. 1-6
    • Singh, J.1    Thornton, J.M.2
  • 31
    • 0025878347 scopus 로고
    • π-π Interactions: The geometry and energetics of phenylalanine-phenylalanine interactions in proteins
    • Hunter C., Singh J., Thornton J. π-π Interactions: the geometry and energetics of phenylalanine-phenylalanine interactions in proteins. J. Mol. Biol. 218:1991;837-846.
    • (1991) J. Mol. Biol. , vol.218 , pp. 837-846
    • Hunter, C.1    Singh, J.2    Thornton, J.3
  • 32
    • 0033179780 scopus 로고    scopus 로고
    • Packing of aromatic rings against tryptophan residues in proteins
    • Samanta U., Debnath P., Chakrabarti P. Packing of aromatic rings against tryptophan residues in proteins. Acta Crystallogr., D. 55:1999;1421-1427.
    • (1999) Acta Crystallogr., D , vol.55 , pp. 1421-1427
    • Samanta, U.1    Debnath, P.2    Chakrabarti, P.3
  • 33
    • 0034651772 scopus 로고    scopus 로고
    • Environment of tryptophan side chains in proteins
    • Samanta U., Debnath P., Chakrabarti P. Environment of tryptophan side chains in proteins. Proteins. 38:2000;288-300.
    • (2000) Proteins , vol.38 , pp. 288-300
    • Samanta, U.1    Debnath, P.2    Chakrabarti, P.3
  • 34
    • 0036216060 scopus 로고    scopus 로고
    • Aromatic-aromatic interactions in and around α-helices
    • Bhattacharyya R., Samanta U., Chakrabarti P. Aromatic-aromatic interactions in and around α-helices. Protein Eng. 15:2002;91-100.
    • (2002) Protein Eng. , vol.15 , pp. 91-100
    • Bhattacharyya, R.1    Samanta, U.2    Chakrabarti, P.3
  • 35
    • 0032546782 scopus 로고    scopus 로고
    • Pi-Stacking interactions. Alive and well in proteins
    • McGaughey G.B., Gagne M., Rappe A.K. pi-Stacking interactions. Alive and well in proteins. J. Biol. Chem. 273:1998;15458-15463.
    • (1998) J. Biol. Chem. , vol.273 , pp. 15458-15463
    • McGaughey, G.B.1    Gagne, M.2    Rappe, A.K.3
  • 36
    • 0036721415 scopus 로고    scopus 로고
    • Aromatic side-chain interactions in proteins: II. Near- and far-sequence Phe-X pairs
    • Thomas A., Meurisse R., Brasseur R. Aromatic side-chain interactions in proteins: II. Near- and far-sequence Phe-X pairs. Proteins. 48:2002;635-644.
    • (2002) Proteins , vol.48 , pp. 635-644
    • Thomas, A.1    Meurisse, R.2    Brasseur, R.3
  • 37
    • 0036721382 scopus 로고    scopus 로고
    • Aromatic side-chain interactions in proteins: I. Main structural features
    • Thomas A., Meurisse R., Charloteaux B., Brasseur R. Aromatic side-chain interactions in proteins: I. Main structural features. Proteins. 48:2002;628-634.
    • (2002) Proteins , vol.48 , pp. 628-634
    • Thomas, A.1    Meurisse, R.2    Charloteaux, B.3    Brasseur, R.4
  • 38
    • 0033406884 scopus 로고    scopus 로고
    • Prediction of protein secondary structure content
    • Liu W.-M., Chou K.-C. Prediction of protein secondary structure content. Protein Eng. 12:1999;1041-1050.
    • (1999) Protein Eng. , vol.12 , pp. 1041-1050
    • Liu, W.-M.1    Chou, K.-C.2
  • 39
    • 0035314074 scopus 로고    scopus 로고
    • PEX, analytical tools for PDB files: I. Pex, analytical tools for PDB files. I. GF-Pex: The basic file to describe a protein
    • Thomas A., Bouffioux O., Geeurickx D., Brasseur R. PEX, analytical tools for PDB files: I. Pex, analytical tools for PDB files. I. GF-Pex: the basic file to describe a protein. Proteins. 43:2001;28-36.
    • (2001) Proteins , vol.43 , pp. 28-36
    • Thomas, A.1    Bouffioux, O.2    Geeurickx, D.3    Brasseur, R.4
  • 40
    • 0015866154 scopus 로고
    • Environment and exposure to solvent of protein atoms. Lysozyme and insulin
    • Shrake A., Rupley J.A. Environment and exposure to solvent of protein atoms. Lysozyme and insulin. J. Mol. Biol. 79:1973;351-371.
    • (1973) J. Mol. Biol. , vol.79 , pp. 351-371
    • Shrake, A.1    Rupley, J.A.2
  • 41
    • 0029055313 scopus 로고
    • Linus: A hierarchical procedure to predict the fold of a protein
    • Srinivasan R., Rose G.D. Linus: a hierarchical procedure to predict the fold of a protein. Proteins. 22:1995;81-99.
    • (1995) Proteins , vol.22 , pp. 81-99
    • Srinivasan, R.1    Rose, G.D.2


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