메뉴 건너뛰기




Volumn 3, Issue 7, 1996, Pages 519-524

Accommodating structurally diverse peptides in proteins

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALIA;

EID: 0030198810     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-5521(96)90141-6     Document Type: Short Survey
Times cited : (12)

References (23)
  • 2
    • 0027853007 scopus 로고
    • Peptide-protein interactions: An overview
    • Zvelebil, M.J.J.M. & Thornton, J.M. (1993). Peptide-protein interactions: an overview. Q. Rev. Biophys. 26, 333-363.
    • (1993) Q. Rev. Biophys. , vol.26 , pp. 333-363
    • Zvelebil, M.J.J.M.1    Thornton, J.M.2
  • 3
    • 0000548829 scopus 로고
    • Three-dimensional structure of peptide-protein complexes: Implications for recognition
    • Marshall, G.R. (1992). Three-dimensional structure of peptide-protein complexes: implications for recognition. Curr. Opin Struct. Biol. 2, 904-909.
    • (1992) Curr. Opin Struct. Biol. , vol.2 , pp. 904-909
    • Marshall, G.R.1
  • 4
    • 0028773294 scopus 로고
    • Antigenic peptide binding by class I and class II histocompatibility proteins
    • Stern, L.J. & Wiley, D.C. (1994). Antigenic peptide binding by class I and class II histocompatibility proteins. Structure 2, 245-251.
    • (1994) Structure , vol.2 , pp. 245-251
    • Stern, L.J.1    Wiley, D.C.2
  • 5
    • 0027525106 scopus 로고
    • The antigenic identity of peptide-MHC complexes: A comparison of the conformations of five viral peptides presented by HLA-A2
    • Madden, D.R., Garboczi, D.N. & Wiley, D.C. (1993). The antigenic identity of peptide-MHC complexes: a comparison of the conformations of five viral peptides presented by HLA-A2. Cell 75, 693-708.
    • (1993) Cell , vol.75 , pp. 693-708
    • Madden, D.R.1    Garboczi, D.N.2    Wiley, D.C.3
  • 6
    • 0026618817 scopus 로고
    • Different length peptides bind to HLA-Aw68 similarly at their ends but bulge out in the middle
    • Quo, H-C., et al., & Wiley, D.C. (1992). Different length peptides bind to HLA-Aw68 similarly at their ends but bulge out in the middle. Nature 360, 364-366.
    • (1992) Nature , vol.360 , pp. 364-366
    • Quo, H.-C.1    Wiley, D.C.2
  • 7
    • 0028987213 scopus 로고
    • b-ovalbumin peptide complex reveals the interplay of primary and secondary anchor positions in the major histocompatibility complex binding groove
    • b-ovalbumin peptide complex reveals the interplay of primary and secondary anchor positions in the major histocompatibility complex binding groove. Proc. Natl. Acad. Sci. USA 92, 2479-2483.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2479-2483
    • Fremont, D.H.1    Stura, E.A.2    Matsumura, M.3    Peterson, P.A.4    Wilson, I.A.5
  • 8
    • 0030069683 scopus 로고    scopus 로고
    • Crystallographic analysis of endogenous peptides associated with HLA-DR1 suggests a common, polyproline-II-like conformation for bound peptides
    • Jardetzky, T.S., et al., & Wiley, D.C. (1996). Crystallographic analysis of endogenous peptides associated with HLA-DR1 suggests a common, polyproline-II-like conformation for bound peptides. Proc. Natl. Acad. Sci. USA 93, 734-738.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 734-738
    • Jardetzky, T.S.1    Wiley, D.C.2
  • 9
    • 0028452862 scopus 로고
    • The structural basis of sequence-independent peptide binding by OppA protein
    • Tame, J.R.H., et al., & Wilkinson, A.J. (1994). The structural basis of sequence-independent peptide binding by OppA protein. Science 264, 1578-1581.
    • (1994) Science , vol.264 , pp. 1578-1581
    • Tame, J.R.H.1    Wilkinson, A.J.2
  • 10
    • 0029646113 scopus 로고
    • The crystal structures of the oligopeptide-binding protein OppA complexed with tripeptide and tetrapeptide ligands
    • Tame, J.R.H., Dodson, E.J., Murshudov, G., Higgins, C.F. & Wilkinson, AJ. (1995). The crystal structures of the oligopeptide-binding protein OppA complexed with tripeptide and tetrapeptide ligands. Structure 3, 1395-1406.
    • (1995) Structure , vol.3 , pp. 1395-1406
    • Tame, J.R.H.1    Dodson, E.J.2    Murshudov, G.3    Higgins, C.F.4    Wilkinson, A.J.5
  • 11
    • 0028786979 scopus 로고
    • Crystal structure of the dipeptide binding protein from Escherichia coli involved in active transport and chemotaxis
    • Dunten, P. & Mowbray, S.L. (1995). Crystal structure of the dipeptide binding protein from Escherichia coli involved in active transport and chemotaxis. Protein Sci. 4, 2327-2334.
    • (1995) Protein Sci. , vol.4 , pp. 2327-2334
    • Dunten, P.1    Mowbray, S.L.2
  • 12
    • 0029200246 scopus 로고
    • 2 Å structure of DppA, a periplasmic dipeptide/transport chemosensory receptor
    • Nickitenko, A.V., Trakhanov, S. & Quiocho, F.A. (1995). 2 Å structure of DppA, a periplasmic dipeptide/transport chemosensory receptor. Biochemistry 34, 16585-16595.
    • (1995) Biochemistry , vol.34 , pp. 16585-16595
    • Nickitenko, A.V.1    Trakhanov, S.2    Quiocho, F.A.3
  • 13
    • 0000319698 scopus 로고
    • Atomic structures and function of periplasmic receptors for active transport and chemotaxis
    • Quiocho, F.A. (1991). Atomic structures and function of periplasmic receptors for active transport and chemotaxis. Curr. Opin. Struct. Biol. 1, 922-933.
    • (1991) Curr. Opin. Struct. Biol. , vol.1 , pp. 922-933
    • Quiocho, F.A.1
  • 14
    • 0026536335 scopus 로고
    • Solution structure of a calmodulin-target peptide complex by multidimensional NMR
    • Ikura, M., Clore, G.M., Gronenborn, A.M., Zhu, G., Klee, C.B. & Bax, A. (1992). Solution structure of a calmodulin-target peptide complex by multidimensional NMR. Science 256, 632-638.
    • (1992) Science , vol.256 , pp. 632-638
    • Ikura, M.1    Clore, G.M.2    Gronenborn, A.M.3    Zhu, G.4    Klee, C.B.5    Bax, A.6
  • 15
    • 0027759276 scopus 로고
    • Modulation of calmodulin plasticity in molecular recognition on the basis of X-ray structures
    • Meador, W.E., Means, A.R. & Quiocho, F.A. (1993). Modulation of calmodulin plasticity in molecular recognition on the basis of X-ray structures. Science 262, 1718-1721.
    • (1993) Science , vol.262 , pp. 1718-1721
    • Meador, W.E.1    Means, A.R.2    Quiocho, F.A.3
  • 16
    • 0028799021 scopus 로고
    • X-ray analysis reveals conformational adaptation of the linker in functional calmodulin mutants
    • Meador, W.E., George, S.E., Means, A.R. & Quiocho, F.A. (1995). X-ray analysis reveals conformational adaptation of the linker in functional calmodulin mutants. Nat. Struct. Biol. 2, 943-945.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 943-945
    • Meador, W.E.1    George, S.E.2    Means, A.R.3    Quiocho, F.A.4
  • 17
    • 0028124954 scopus 로고
    • Investigating the high affinity and low sequence specificity of calmodulin binding to its targets
    • Afshar, M., et al., & Haiech, J. (1994). Investigating the high affinity and low sequence specificity of calmodulin binding to its targets. J. Mol. Biol. 244, 554-571.
    • (1994) J. Mol. Biol. , vol.244 , pp. 554-571
    • Afshar, M.1    Haiech, J.2
  • 18
    • 0030002422 scopus 로고    scopus 로고
    • Alanine substitutions in calmodulin-binding peptides result in unexpected affinity enhancement
    • Montigiani, S., Neri, G., Neri, P. & Neri, D. (1996). Alanine substitutions in calmodulin-binding peptides result in unexpected affinity enhancement. J. Mol. Biol. 258, 6-13.
    • (1996) J. Mol. Biol. , vol.258 , pp. 6-13
    • Montigiani, S.1    Neri, G.2    Neri, P.3    Neri, D.4
  • 21
    • 0027962645 scopus 로고
    • Two binding orientations to the Src SH3 domain: Development of a general model for SH3-ligand interactions
    • Feng, S., Chen, J.K., Yu, H., Simon, J.A. & Schreiber, S.L. (1994). Two binding orientations to the Src SH3 domain: development of a general model for SH3-ligand interactions. Science 266, 1241-1246.
    • (1994) Science , vol.266 , pp. 1241-1246
    • Feng, S.1    Chen, J.K.2    Yu, H.3    Simon, J.A.4    Schreiber, S.L.5
  • 22
    • 0028148629 scopus 로고
    • Structural determinants of peptide-binding orientation and of sequence specificity in SH3 domains
    • Lim, W.A, Richards, F.M. & Fox, R.O. (1994). Structural determinants of peptide-binding orientation and of sequence specificity in SH3 domains. Nature 372, 375-379.
    • (1994) Nature , vol.372 , pp. 375-379
    • Lim, W.A.1    Richards, F.M.2    Fox, R.O.3
  • 23
    • 0029980671 scopus 로고    scopus 로고
    • Crystal structure of PI3K SH3 domain at 2.0 Å resolution
    • Liang, J., Chen, J.K., Schreiber, S.L. & Clardy, J. (1996). Crystal structure of PI3K SH3 domain at 2.0 Å resolution. J. Mol. Biol. 257, 632-643.
    • (1996) J. Mol. Biol. , vol.257 , pp. 632-643
    • Liang, J.1    Chen, J.K.2    Schreiber, S.L.3    Clardy, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.