메뉴 건너뛰기




Volumn 377, Issue 4, 2008, Pages 1251-1264

A Logical OR Redundancy within the Asx-Pro-Asx-Gly Type I β-Turn Motif

Author keywords

protein engineering; protein evolution; protein folding; protein stability; hairpin

Indexed keywords

ALANINE; ASPARAGINE; ASPARTIC ACID; FIBROBLAST GROWTH FACTOR 1; GLYCINE; LEUCINE; MUTANT PROTEIN; PROLINE;

EID: 40849089197     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.01.055     Document Type: Article
Times cited : (25)

References (37)
  • 1
    • 0019443447 scopus 로고
    • The anatomy and taxonomy of protein structure
    • Richardson J.S. The anatomy and taxonomy of protein structure. Adv. Protein Chem. 34 (1981) 167-339
    • (1981) Adv. Protein Chem. , vol.34 , pp. 167-339
    • Richardson, J.S.1
  • 2
    • 0024391832 scopus 로고
    • Conformation of β-hairpins in protein structures. A systematic classification with applications to modelling by homology, electron density fitting and protein engineering
    • Sibanda B.L., Blundell T.L., and Thornton J.M. Conformation of β-hairpins in protein structures. A systematic classification with applications to modelling by homology, electron density fitting and protein engineering. J. Mol. Biol. 206 (1989) 759-777
    • (1989) J. Mol. Biol. , vol.206 , pp. 759-777
    • Sibanda, B.L.1    Blundell, T.L.2    Thornton, J.M.3
  • 3
    • 0031455857 scopus 로고    scopus 로고
    • Beta-hairpins in proteins revisited: lessons for de novo design
    • Gunasekaran K., Ramakrishnan C., and Balaram P. Beta-hairpins in proteins revisited: lessons for de novo design. Protein Eng. 10 (1997) 1131-1141
    • (1997) Protein Eng. , vol.10 , pp. 1131-1141
    • Gunasekaran, K.1    Ramakrishnan, C.2    Balaram, P.3
  • 4
    • 0028566270 scopus 로고
    • A revised set of potentials for beta-turn formation in proteins
    • Hutchinson E.G., and Thornton J.M. A revised set of potentials for beta-turn formation in proteins. Protein Sci. 3 (1994) 2207-2216
    • (1994) Protein Sci. , vol.3 , pp. 2207-2216
    • Hutchinson, E.G.1    Thornton, J.M.2
  • 5
    • 0033752859 scopus 로고    scopus 로고
    • β- and γ-turns in proteins revisited: a new set of amino acid turn-type dependent positional preferences and potentials
    • Guruprasad K., and Rajkumar S. β- and γ-turns in proteins revisited: a new set of amino acid turn-type dependent positional preferences and potentials. J. Biosci. 25 (2000) 143-156
    • (2000) J. Biosci. , vol.25 , pp. 143-156
    • Guruprasad, K.1    Rajkumar, S.2
  • 6
    • 0037304420 scopus 로고    scopus 로고
    • Turn stability in β-hairpin peptides: investigation of peptides containing 3:5 type I G1 bulge turns
    • Blandl T., Cochran A.G., and Skelton N.J. Turn stability in β-hairpin peptides: investigation of peptides containing 3:5 type I G1 bulge turns. Protein Sci. 12 (2003) 237-247
    • (2003) Protein Sci. , vol.12 , pp. 237-247
    • Blandl, T.1    Cochran, A.G.2    Skelton, N.J.3
  • 7
    • 0033548459 scopus 로고    scopus 로고
    • A natural grouping of motifs with an aspartate or asparagine residue forming two hydrogen bonds to residues ahead in sequence: their occurrence at a-helical N termini and in other situations
    • Wan W.-Y., and Milner-White E.J. A natural grouping of motifs with an aspartate or asparagine residue forming two hydrogen bonds to residues ahead in sequence: their occurrence at a-helical N termini and in other situations. J. Mol. Biol. 286 (1999) 1633-1649
    • (1999) J. Mol. Biol. , vol.286 , pp. 1633-1649
    • Wan, W.-Y.1    Milner-White, E.J.2
  • 8
    • 1842403587 scopus 로고    scopus 로고
    • Turn residue sequence determines beta-hairpin conformation in designed peptides
    • de Alba E., Jimenez M.A., and Rico M. Turn residue sequence determines beta-hairpin conformation in designed peptides. J. Am. Chem. Soc. 119 (1997) 175-183
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 175-183
    • de Alba, E.1    Jimenez, M.A.2    Rico, M.3
  • 9
    • 4544361664 scopus 로고    scopus 로고
    • Beta-hairpin folding and stability: molecular dynamics simulations of designed peptides in aqueous solution
    • Santiveri C.M., Jimenez M.A., Rico M., Van Gunsteren W.F., and Daura X. Beta-hairpin folding and stability: molecular dynamics simulations of designed peptides in aqueous solution. J. Pept. Sci. 10 (2004) 546-565
    • (2004) J. Pept. Sci. , vol.10 , pp. 546-565
    • Santiveri, C.M.1    Jimenez, M.A.2    Rico, M.3    Van Gunsteren, W.F.4    Daura, X.5
  • 10
    • 1842611349 scopus 로고    scopus 로고
    • Factors involved in the stability of isolated beta-sheets: turn sequence, beta-sheet twisting, and hydrophobic surface burial
    • Santiveri C.M., Santoro J., Rico M., and Jimenez M.A. Factors involved in the stability of isolated beta-sheets: turn sequence, beta-sheet twisting, and hydrophobic surface burial. Protein Sci. 13 (2004) 1134-1147
    • (2004) Protein Sci. , vol.13 , pp. 1134-1147
    • Santiveri, C.M.1    Santoro, J.2    Rico, M.3    Jimenez, M.A.4
  • 11
    • 0030334822 scopus 로고    scopus 로고
    • Conformational investigations of designed short linear peptides able to fold into beta-hairpin structures in aqueous solution
    • de Alba E., Jimenez M.A., Rico M., and Nieto J.L. Conformational investigations of designed short linear peptides able to fold into beta-hairpin structures in aqueous solution. Fold. Des. 1 (1996) 133-144
    • (1996) Fold. Des. , vol.1 , pp. 133-144
    • de Alba, E.1    Jimenez, M.A.2    Rico, M.3    Nieto, J.L.4
  • 12
    • 0034489543 scopus 로고    scopus 로고
    • Structural characterization of a mutant peptide derived from ubiquitin: implications for protein folding
    • Zerella R., Chen P.Y., Evans P.A., Raine A., and Williams D.H. Structural characterization of a mutant peptide derived from ubiquitin: implications for protein folding. Protein Sci. 9 (2000) 2142-2150
    • (2000) Protein Sci. , vol.9 , pp. 2142-2150
    • Zerella, R.1    Chen, P.Y.2    Evans, P.A.3    Raine, A.4    Williams, D.H.5
  • 14
    • 0026556882 scopus 로고
    • β-Trefoil fold. Patterns of structure and sequence in the Kunitz inhibitors interleukins-1β and 1α and fibroblast growth factors
    • Murzin A.G., Lesk A.M., and Chothia C. β-Trefoil fold. Patterns of structure and sequence in the Kunitz inhibitors interleukins-1β and 1α and fibroblast growth factors. J. Mol. Biol. 223 (1992) 531-543
    • (1992) J. Mol. Biol. , vol.223 , pp. 531-543
    • Murzin, A.G.1    Lesk, A.M.2    Chothia, C.3
  • 15
    • 0030031438 scopus 로고    scopus 로고
    • X-ray crystal structure of human acidic fibroblast growth factor
    • Blaber M., DiSalvo J., and Thomas K.A. X-ray crystal structure of human acidic fibroblast growth factor. Biochemistry 35 (1996) 2086-2094
    • (1996) Biochemistry , vol.35 , pp. 2086-2094
    • Blaber, M.1    DiSalvo, J.2    Thomas, K.A.3
  • 16
    • 0033635299 scopus 로고    scopus 로고
    • Crystal structure of a ternary FGF-FGFR-heparin complex reveals a dual role for heparin in FGFR binding and dimerization
    • Schlessinger J., Plotnikov A.N., Ibrahimi O.A., Eliseenkova A.V., Yeh B.K., Yayon A., et al. Crystal structure of a ternary FGF-FGFR-heparin complex reveals a dual role for heparin in FGFR binding and dimerization. Mol. Cell. Biol. 6 (2000) 743-750
    • (2000) Mol. Cell. Biol. , vol.6 , pp. 743-750
    • Schlessinger, J.1    Plotnikov, A.N.2    Ibrahimi, O.A.3    Eliseenkova, A.V.4    Yeh, B.K.5    Yayon, A.6
  • 17
    • 0034718796 scopus 로고    scopus 로고
    • Crystal structure of fibroblast growth factor receptor ectodomain bound to ligand and heparin
    • Pellegrini L., Burke D.F., von Delft F., Mulloy B., and Blundell T.L. Crystal structure of fibroblast growth factor receptor ectodomain bound to ligand and heparin. Nature 407 (2000) 1029-1034
    • (2000) Nature , vol.407 , pp. 1029-1034
    • Pellegrini, L.1    Burke, D.F.2    von Delft, F.3    Mulloy, B.4    Blundell, T.L.5
  • 18
    • 34447092609 scopus 로고    scopus 로고
    • Spackling the crack: stabilizing human fibroblast growth factor-1 by targeting the N- and C-terminus β-strand interactions
    • Dubey V.K., Lee J., Somasundaram T., Blaber S., and Blaber M. Spackling the crack: stabilizing human fibroblast growth factor-1 by targeting the N- and C-terminus β-strand interactions. J. Mol. Biol. 371 (2007) 256-268
    • (2007) J. Mol. Biol. , vol.371 , pp. 256-268
    • Dubey, V.K.1    Lee, J.2    Somasundaram, T.3    Blaber, S.4    Blaber, M.5
  • 19
    • 0002846347 scopus 로고    scopus 로고
    • Measuring the conformational stability of a protein
    • Creighton T.E. (Ed), Oxford University Press, Oxford
    • Pace C.N., and Scholtz J.M. Measuring the conformational stability of a protein. In: Creighton T.E. (Ed). Protein Structure: A Practical Approach (1997), Oxford University Press, Oxford 299-321
    • (1997) Protein Structure: A Practical Approach , pp. 299-321
    • Pace, C.N.1    Scholtz, J.M.2
  • 20
    • 0037427477 scopus 로고    scopus 로고
    • Identification of a key structural element for protein folding within β-hairpin turns
    • Kim J., Brych S.R., Lee J., Logan T.M., and Blaber M. Identification of a key structural element for protein folding within β-hairpin turns. J. Mol. Biol. 328 (2003) 951-961
    • (2003) J. Mol. Biol. , vol.328 , pp. 951-961
    • Kim, J.1    Brych, S.R.2    Lee, J.3    Logan, T.M.4    Blaber, M.5
  • 21
    • 0035187229 scopus 로고    scopus 로고
    • Structure and stability effects of mutations designed to increase the primary sequence symmetry within the core region of a β-trefoil
    • Brych S.R., Blaber S.I., Logan T.M., and Blaber M. Structure and stability effects of mutations designed to increase the primary sequence symmetry within the core region of a β-trefoil. Protein Sci. 10 (2001) 2587-2599
    • (2001) Protein Sci. , vol.10 , pp. 2587-2599
    • Brych, S.R.1    Blaber, S.I.2    Logan, T.M.3    Blaber, M.4
  • 22
    • 0026511656 scopus 로고
    • The folding of an enzyme: I. Theory of protein engineering analysis of stability and pathway of protein folding
    • Fersht A.R., Matouschek A., and Serrano L. The folding of an enzyme: I. Theory of protein engineering analysis of stability and pathway of protein folding. J. Mol. Biol. 224 (1992) 771-782
    • (1992) J. Mol. Biol. , vol.224 , pp. 771-782
    • Fersht, A.R.1    Matouschek, A.2    Serrano, L.3
  • 23
    • 33745618137 scopus 로고    scopus 로고
    • φ{symbol}-Analysis of the folding of the B domain of protein A using multiple optical probes
    • Sato S., Religa T.L., and Fersht A.R. φ{symbol}-Analysis of the folding of the B domain of protein A using multiple optical probes. J. Mol. Biol. 360 (2006) 850-864
    • (2006) J. Mol. Biol. , vol.360 , pp. 850-864
    • Sato, S.1    Religa, T.L.2    Fersht, A.R.3
  • 24
    • 0033012341 scopus 로고    scopus 로고
    • Reversible thermal denaturation of human FGF-1 induced by low concentrations of guanidine hydrochloride
    • Blaber S.I., Culajay J.F., Khurana A., and Blaber M. Reversible thermal denaturation of human FGF-1 induced by low concentrations of guanidine hydrochloride. Biophys. J. 77 (1999) 470-477
    • (1999) Biophys. J. , vol.77 , pp. 470-477
    • Blaber, S.I.1    Culajay, J.F.2    Khurana, A.3    Blaber, M.4
  • 25
    • 0034691318 scopus 로고    scopus 로고
    • Thermodynamic characterization of mutants of human fibroblast growth factor 1 with an increased physiological half-life
    • Culajay J.F., Blaber S.I., Khurana A., and Blaber M. Thermodynamic characterization of mutants of human fibroblast growth factor 1 with an increased physiological half-life. Biochemistry 39 (2000) 7153-7158
    • (2000) Biochemistry , vol.39 , pp. 7153-7158
    • Culajay, J.F.1    Blaber, S.I.2    Khurana, A.3    Blaber, M.4
  • 26
    • 0022512063 scopus 로고
    • The complete amino acid sequence of human brain-derived acidic fibroblast growth factor
    • Gimenez-Gallego G., Conn G., Hatcher V.B., and Thomas K.A. The complete amino acid sequence of human brain-derived acidic fibroblast growth factor. Biochem. Biophys. Res. Commun. 128 (1986) 611-617
    • (1986) Biochem. Biophys. Res. Commun. , vol.128 , pp. 611-617
    • Gimenez-Gallego, G.1    Conn, G.2    Hatcher, V.B.3    Thomas, K.A.4
  • 27
    • 0025671885 scopus 로고
    • Disulfide bonds are neither required, present, nor compatible with full activity of human recombinant acidic fibroblast growth factor
    • Linemeyer D.L., Menke J.G., Kelly L.J., Disalvo J., Soderman D., Schaeffer M.-T., et al. Disulfide bonds are neither required, present, nor compatible with full activity of human recombinant acidic fibroblast growth factor. Growth Factors 3 (1990) 287-298
    • (1990) Growth Factors , vol.3 , pp. 287-298
    • Linemeyer, D.L.1    Menke, J.G.2    Kelly, L.J.3    Disalvo, J.4    Soderman, D.5    Schaeffer, M.-T.6
  • 28
    • 0026009380 scopus 로고
    • Conversion of cysteine to serine residues alters the activity, stability, and heparin dependence of acidic fibroblast growth factor
    • Ortega S., Schaeffer M.-T., Soderman D., DiSalvo J., Linemeyer D.L., Gimenez-Gallego G., and Thomas K.A. Conversion of cysteine to serine residues alters the activity, stability, and heparin dependence of acidic fibroblast growth factor. J. Biol. Chem. 266 (1991) 5842-5846
    • (1991) J. Biol. Chem. , vol.266 , pp. 5842-5846
    • Ortega, S.1    Schaeffer, M.-T.2    Soderman, D.3    DiSalvo, J.4    Linemeyer, D.L.5    Gimenez-Gallego, G.6    Thomas, K.A.7
  • 30
    • 0345276586 scopus 로고    scopus 로고
    • Accommodation of a highly symmetric core within a symmetric protein superfold
    • Brych S.R., Kim J., Logan T.M., and Blaber M. Accommodation of a highly symmetric core within a symmetric protein superfold. Protein Sci. 12 (2003) 2704-2718
    • (2003) Protein Sci. , vol.12 , pp. 2704-2718
    • Brych, S.R.1    Kim, J.2    Logan, T.M.3    Blaber, M.4
  • 31
    • 0027958069 scopus 로고
    • The use of fluorescence methods to monitor unfolding transitions in proteins
    • Eftink M.R. The use of fluorescence methods to monitor unfolding transitions in proteins. Biophys. J. 66 (1994) 482-501
    • (1994) Biophys. J. , vol.66 , pp. 482-501
    • Eftink, M.R.1
  • 34
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 36
    • 84889120137 scopus 로고
    • Improved methods for the building of protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zou J.Y., Cowan S.W., and Kjeldgaard M. Improved methods for the building of protein models in electron density maps and the location of errors in these models. Acta Crystallogr. Sect. A 47 (1991) 110-119
    • (1991) Acta Crystallogr. Sect. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 37
    • 0026597444 scopus 로고
    • Free R value: a novel statistical quantity for assessing the accuracy of crystal structures
    • Brunger A.T. Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 355 (1992) 472-475
    • (1992) Nature , vol.355 , pp. 472-475
    • Brunger, A.T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.