메뉴 건너뛰기




Volumn 378, Issue 2, 2008, Pages 459-467

High-Resolution Structure of a Self-Assembly-Competent Form of a Hydrophobic Peptide Captured in a Soluble β-Sheet Scaffold

Author keywords

amyloid fibril; protein engineering; single layer sheet; solubilization; x ray crystallography

Indexed keywords

BACTERIAL ANTIGEN; ILE5 PEPTIDE; OLIGOPEPTIDE; OUTER SURFACE PROTEIN; SCAFFOLD PROTEIN; UNCLASSIFIED DRUG;

EID: 41249083889     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.02.051     Document Type: Article
Times cited : (14)

References (36)
  • 1
    • 0037317334 scopus 로고    scopus 로고
    • Protein folding and disease: a view from the first Horizon Symposium
    • Dobson C.M. Protein folding and disease: a view from the first Horizon Symposium. Nat. Rev. Drug Discov. 2 (2003) 154-160
    • (2003) Nat. Rev. Drug Discov. , vol.2 , pp. 154-160
    • Dobson, C.M.1
  • 2
    • 4143141192 scopus 로고    scopus 로고
    • Self-assembling peptides and proteins for nanotechnological applications
    • Rajagopal K., and Schneider J.P. Self-assembling peptides and proteins for nanotechnological applications. Curr. Opin. Struct. Biol. 14 (2004) 480-486
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 480-486
    • Rajagopal, K.1    Schneider, J.P.2
  • 4
    • 1642433249 scopus 로고    scopus 로고
    • High-resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopy
    • Jaroniec C.P., MacPhee C.E., Bajaj V.S., McMahon M.T., Dobson C.M., and Griffin R.G. High-resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopy. Proc. Natl Acad. Sci. USA 101 (2004) 711-716
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 711-716
    • Jaroniec, C.P.1    MacPhee, C.E.2    Bajaj, V.S.3    McMahon, M.T.4    Dobson, C.M.5    Griffin, R.G.6
  • 6
    • 30744433878 scopus 로고    scopus 로고
    • Experimental constraints on quaternary structure in Alzheimer's beta-amyloid fibrils
    • Petkova A.T., Yau W.M., and Tycko R. Experimental constraints on quaternary structure in Alzheimer's beta-amyloid fibrils. Biochemistry 45 (2006) 498-512
    • (2006) Biochemistry , vol.45 , pp. 498-512
    • Petkova, A.T.1    Yau, W.M.2    Tycko, R.3
  • 7
    • 1342324027 scopus 로고    scopus 로고
    • Progress towards a molecular-level structural understanding of amyloid fibrils
    • Tycko R. Progress towards a molecular-level structural understanding of amyloid fibrils. Curr. Opin. Struct. Biol. 14 (2004) 96-103
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 96-103
    • Tycko, R.1
  • 10
    • 33746800825 scopus 로고    scopus 로고
    • Molecular dynamics analyses of cross-β-spine steric zipper models: β-sheet twisting and aggregation
    • Esposito L., Pedone C., and Vitagliano L. Molecular dynamics analyses of cross-β-spine steric zipper models: β-sheet twisting and aggregation. Proc. Natl Acad. Sci. USA 103 (2006) 11533-11538
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 11533-11538
    • Esposito, L.1    Pedone, C.2    Vitagliano, L.3
  • 11
    • 0029059477 scopus 로고
    • Incorporation of glutamine repeats makes protein oligomerize: implications for neurodegenerative diseases
    • Stott K., Blackburn J.M., Butler P.J., and Perutz M. Incorporation of glutamine repeats makes protein oligomerize: implications for neurodegenerative diseases. Proc. Natl Acad. Sci. USA 92 (1995) 6509-6513
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 6509-6513
    • Stott, K.1    Blackburn, J.M.2    Butler, P.J.3    Perutz, M.4
  • 12
    • 0000522537 scopus 로고    scopus 로고
    • Crystal structure of a dimeric chymotrypsin inhibitor 2 mutant containing an inserted glutamine repeat
    • Chen Y.W., Stott K., and Perutz M.F. Crystal structure of a dimeric chymotrypsin inhibitor 2 mutant containing an inserted glutamine repeat. Proc. Natl Acad. Sci. USA 96 (1999) 1257-1261
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 1257-1261
    • Chen, Y.W.1    Stott, K.2    Perutz, M.F.3
  • 15
    • 33947314274 scopus 로고    scopus 로고
    • Hydrophobic surface burial is the major stability determinant of a flat, single-layer beta-sheet
    • Yan S., Gawlak G., Makabe K., Tereshko V., Koide A., and Koide S. Hydrophobic surface burial is the major stability determinant of a flat, single-layer beta-sheet. J. Mol. Biol. 368 (2007) 230-243
    • (2007) J. Mol. Biol. , vol.368 , pp. 230-243
    • Yan, S.1    Gawlak, G.2    Makabe, K.3    Tereshko, V.4    Koide, A.5    Koide, S.6
  • 16
    • 0034636976 scopus 로고    scopus 로고
    • Solution conformation and amyloid-like fibril formation of a polar peptide derived from a β-hairpin in the OspA single-layer β-sheet
    • Ohnishi S., Koide A., and Koide S. Solution conformation and amyloid-like fibril formation of a polar peptide derived from a β-hairpin in the OspA single-layer β-sheet. J. Mol. Biol. 301 (2000) 477-489
    • (2000) J. Mol. Biol. , vol.301 , pp. 477-489
    • Ohnishi, S.1    Koide, A.2    Koide, S.3
  • 17
    • 0034719388 scopus 로고    scopus 로고
    • Design of single-layer beta-sheets without a hydrophobic core
    • Koide S., Huang X., Link K., Koide A., Bu Z., and Engelman D.M. Design of single-layer beta-sheets without a hydrophobic core. Nature 403 (2000) 456-460
    • (2000) Nature , vol.403 , pp. 456-460
    • Koide, S.1    Huang, X.2    Link, K.3    Koide, A.4    Bu, Z.5    Engelman, D.M.6
  • 18
    • 0037022563 scopus 로고    scopus 로고
    • Natural beta-sheet proteins use negative design to avoid edge-to-edge aggregation
    • Richardson J.S., and Richardson D.C. Natural beta-sheet proteins use negative design to avoid edge-to-edge aggregation. Proc. Natl Acad. Sci. USA 99 (2002) 2754-2759
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 2754-2759
    • Richardson, J.S.1    Richardson, D.C.2
  • 19
    • 0346057932 scopus 로고    scopus 로고
    • Increasing the amphiphilicity of an amyloidogenic peptide changes the beta-sheet structure in the fibrils from antiparallel to parallel
    • Gordon D.J., Balbach J.J., Tycko R., and Meredith S.C. Increasing the amphiphilicity of an amyloidogenic peptide changes the beta-sheet structure in the fibrils from antiparallel to parallel. Biophys. J. 86 (2004) 428-434
    • (2004) Biophys. J. , vol.86 , pp. 428-434
    • Gordon, D.J.1    Balbach, J.J.2    Tycko, R.3    Meredith, S.C.4
  • 20
    • 0036845354 scopus 로고    scopus 로고
    • The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation
    • Fandrich M., and Dobson C.M. The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation. EMBO J. 21 (2002) 5682-5690
    • (2002) EMBO J. , vol.21 , pp. 5682-5690
    • Fandrich, M.1    Dobson, C.M.2
  • 21
    • 20444403757 scopus 로고    scopus 로고
    • Prediction of "aggregation-prone" and "aggregation-susceptible" regions in proteins associated with neurodegenerative diseases
    • Pawar A.P., Dubay K.F., Zurdo J., Chiti F., Vendruscolo M., and Dobson C.M. Prediction of "aggregation-prone" and "aggregation-susceptible" regions in proteins associated with neurodegenerative diseases. J. Mol. Biol. 350 (2005) 379-392
    • (2005) J. Mol. Biol. , vol.350 , pp. 379-392
    • Pawar, A.P.1    Dubay, K.F.2    Zurdo, J.3    Chiti, F.4    Vendruscolo, M.5    Dobson, C.M.6
  • 22
    • 32344448608 scopus 로고    scopus 로고
    • Protein aggregation and amyloidosis: confusion of the kinds?
    • Rousseau F., Schymkowitz J., and Serrano L. Protein aggregation and amyloidosis: confusion of the kinds?. Curr. Opin. Struct. Biol. 16 (2006) 118-126
    • (2006) Curr. Opin. Struct. Biol. , vol.16 , pp. 118-126
    • Rousseau, F.1    Schymkowitz, J.2    Serrano, L.3
  • 23
    • 0242628911 scopus 로고    scopus 로고
    • Structural transitions involved in a novel amyloid-like beta-sheet assemblage of tripeptide derivatives
    • Ganesh S., and Jayakumar R. Structural transitions involved in a novel amyloid-like beta-sheet assemblage of tripeptide derivatives. Biopolymers 70 (2003) 336-345
    • (2003) Biopolymers , vol.70 , pp. 336-345
    • Ganesh, S.1    Jayakumar, R.2
  • 26
    • 1942457259 scopus 로고    scopus 로고
    • Conformational heterogeneity of an equilibrium folding intermediate quantified and mapped by scanning mutagenesis
    • Yan S., Gawlak G., Smith J., Silver L., Koide A., and Koide S. Conformational heterogeneity of an equilibrium folding intermediate quantified and mapped by scanning mutagenesis. J. Mol. Biol. 338 (2004) 811-825
    • (2004) J. Mol. Biol. , vol.338 , pp. 811-825
    • Yan, S.1    Gawlak, G.2    Smith, J.3    Silver, L.4    Koide, A.5    Koide, S.6
  • 27
    • 33746565309 scopus 로고    scopus 로고
    • Atomic-resolution crystal structure of Borrelia burgdorferi outer surface protein A via surface engineering
    • Makabe K., Tereshko V., Gawlak G., Yan S., and Koide S. Atomic-resolution crystal structure of Borrelia burgdorferi outer surface protein A via surface engineering. Protein Sci. 15 (2006) 1907-1914
    • (2006) Protein Sci. , vol.15 , pp. 1907-1914
    • Makabe, K.1    Tereshko, V.2    Gawlak, G.3    Yan, S.4    Koide, S.5
  • 28
    • 0029058159 scopus 로고
    • An analysis of side chain interactions and pair correlations within antiparallel beta-sheets: the differences between backbone hydrogen-bonded and non-hydrogen-bonded residue pairs
    • Wouters M.A., and Curmi P.M. An analysis of side chain interactions and pair correlations within antiparallel beta-sheets: the differences between backbone hydrogen-bonded and non-hydrogen-bonded residue pairs. Proteins: Struct., Funct., Genet. 22 (1995) 119-131
    • (1995) Proteins: Struct., Funct., Genet. , vol.22 , pp. 119-131
    • Wouters, M.A.1    Curmi, P.M.2
  • 29
    • 0027173033 scopus 로고
    • Weak points of antiparallel beta-sheets. How are they filled up in globular proteins?
    • Finkelstein A.V., and Nakamura H. Weak points of antiparallel beta-sheets. How are they filled up in globular proteins?. Protein Eng. 6 (1993) 367-372
    • (1993) Protein Eng. , vol.6 , pp. 367-372
    • Finkelstein, A.V.1    Nakamura, H.2
  • 30
    • 28044457195 scopus 로고    scopus 로고
    • The amyloid stretch hypothesis: recruiting proteins toward the dark side
    • Esteras-Chopo A., Serrano L., and Lopez de la Paz M. The amyloid stretch hypothesis: recruiting proteins toward the dark side. Proc. Natl Acad. Sci. USA 102 (2005) 16672-16677
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 16672-16677
    • Esteras-Chopo, A.1    Serrano, L.2    Lopez de la Paz, M.3
  • 31
    • 33750430630 scopus 로고    scopus 로고
    • Generic hydrophobic residues are sufficient to promote aggregation of the Alzheimer's Aβ42 peptide
    • Kim W., and Hecht M.H. Generic hydrophobic residues are sufficient to promote aggregation of the Alzheimer's Aβ42 peptide. Proc. Natl Acad. Sci. USA 103 (2006) 15824-15829
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 15824-15829
    • Kim, W.1    Hecht, M.H.2
  • 33
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.