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Volumn 80, Issue 6, 2001, Pages 2912-2921

Plasticity in protein-peptide recognition: Crystal structures of two different peptides bound to concanavalin A

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CARBOHYDRATE; CONCANAVALIN A; OLIGOPEPTIDE; PROTEIN SUBUNIT;

EID: 0035014622     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(01)76256-X     Document Type: Article
Times cited : (26)

References (32)
  • 1
    • 0027686741 scopus 로고
    • Molecular basis of crossreactivity and limits of antibody-antigen complementarity
    • Arevalo, J. H., M. J. Taussig, and I. A. Wilson. 1993. Molecular basis of crossreactivity and limits of antibody-antigen complementarity. Nature. 365:859-863.
    • (1993) Nature , vol.365 , pp. 859-863
    • Arevalo, J.H.1    Taussig, M.J.2    Wilson, I.A.3
  • 2
    • 0024973407 scopus 로고
    • Structural plasticity broadens the specificity of an engineered protease
    • Bone, R., J. L. Silen, and D. Agard. 1989. Structural plasticity broadens the specificity of an engineered protease. Science. 339:191-195.
    • (1989) Science , vol.339 , pp. 191-195
    • Bone, R.1    Silen, J.L.2    Agard, D.3
  • 3
    • 0026597444 scopus 로고
    • The free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, A. T. 1992. The free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature. 355:472-474.
    • (1992) Nature , vol.355 , pp. 472-474
    • Brünger, A.T.1
  • 5
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • CCP4, SERC Daresbury Laboratory, Warrington, W A4 4AD, England. 1994. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D50:760-763.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 760-763
  • 6
    • 0033598941 scopus 로고    scopus 로고
    • The crystal structure of a GroEL/peptide complex: Plasticity as a basis for substrate diversity
    • Chen, L., and P. B. Sigler. 1999. The crystal structure of a GroEL/peptide complex: Plasticity as a basis for substrate diversity. Cell. 99:757-768.
    • (1999) Cell , vol.99 , pp. 757-768
    • Chen, L.1    Sigler, P.B.2
  • 7
    • 0032549142 scopus 로고    scopus 로고
    • Structural basis of plasticity in T cell receptor recognition of a self peptide-MHC antigen
    • Garcia, K. C., M. Degano, L. R. Pease, M. Huang, P. A. Peterson, L. Teyton, and I. A. Wilson. 1998. Structural basis of plasticity in T cell receptor recognition of a self peptide-MHC antigen. Science. 279: 1166-1172.
    • (1998) Science , vol.279 , pp. 1166-1172
    • Garcia, K.C.1    Degano, M.2    Pease, L.R.3    Huang, M.4    Peterson, P.A.5    Teyton, L.6    Wilson, I.A.7
  • 8
    • 0015516458 scopus 로고
    • Structure of concanavalin A at 2.4 Å resolution
    • Hardman, K. D., and C. F. Ainsworth. 1972. Structure of concanavalin A at 2.4 Å resolution. Biochemistry. 11:4910-4919.
    • (1972) Biochemistry , vol.11 , pp. 4910-4919
    • Hardman, K.D.1    Ainsworth, C.F.2
  • 9
    • 0034674266 scopus 로고    scopus 로고
    • Structural basis of functional mimicry between carbohydrate and peptide ligands of ConA
    • Jain, D., K. Kaur, M. Goel, and D. M. Salunke. 2000a. Structural basis of functional mimicry between carbohydrate and peptide ligands of ConA. Biochem. Biophys. Res. Commun. 272:843-849.
    • (2000) Biochem. Biophys. Res. Commun. , vol.272 , pp. 843-849
    • Jain, D.1    Kaur, K.2    Goel, M.3    Salunke, D.M.4
  • 10
    • 0034717303 scopus 로고    scopus 로고
    • Structural and functional consequences of peptide-carbohydrate mimicry
    • Jain, D., K. J. Kaur, B. Sundaravadivel, and D. M. Salunke. 2000b. Structural and functional consequences of peptide-carbohydrate mimicry. J. Biol. Chem. 275:16098-16102.
    • (2000) J. Biol. Chem. , vol.275 , pp. 16098-16102
    • Jain, D.1    Kaur, K.J.2    Sundaravadivel, B.3    Salunke, D.M.4
  • 11
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A., S. Cowan, J. Y. Zou, and M. Kjeldgaard. 1991. Improved methods for building protein models in electron density maps and the location of errors in these models Acta Crystallogr. A47:110-119.
    • (1991) Acta Crystallogr. , vol.A47 , pp. 110-119
    • Jones, T.A.1    Cowan, S.2    Zou, J.Y.3    Kjeldgaard, M.4
  • 12
    • 0028841829 scopus 로고
    • Binding of protein targets of peptidic leads discovered by phage display: Crystal structures of streptavidin-bound linear and cyclic peptide ligands containing the HPQ sequence
    • Katz, B. A. 1995. Binding of protein targets of peptidic leads discovered by phage display: crystal structures of streptavidin-bound linear and cyclic peptide ligands containing the HPQ sequence. Biochemistry. 34: 15421-15429.
    • (1995) Biochemistry , vol.34 , pp. 15421-15429
    • Katz, B.A.1
  • 13
    • 0035972027 scopus 로고    scopus 로고
    • Immunological implications of structural mimicry between a dodecapeptide and a carbohydrate moiety
    • Kaur, K. J., D. Jain, M. Goel, and D. M. Salunke. 2001. Immunological implications of structural mimicry between a dodecapeptide and a carbohydrate moiety. Vaccine. 19:3124-3130.
    • (2001) Vaccine , vol.19 , pp. 3124-3130
    • Kaur, K.J.1    Jain, D.2    Goel, M.3    Salunke, D.M.4
  • 14
    • 0031058735 scopus 로고    scopus 로고
    • Topological analysis of the functional mimicry between a peptide and a carbohydrate moiety
    • Kaur, K. J., S. Khurana, and D. M. Salunke. 1997. Topological analysis of the functional mimicry between a peptide and a carbohydrate moiety. J. Biol. Chem. 272:5539-5543.
    • (1997) J. Biol. Chem. , vol.272 , pp. 5539-5543
    • Kaur, K.J.1    Khurana, S.2    Salunke, D.M.3
  • 15
    • 0031454829 scopus 로고    scopus 로고
    • Crystallographic analysis of anti-p24 (HIV-I) monoclonal antibody cross-reactivity and polyspecificity
    • Keitel, T., A. Kramer, H. Wessner, C. Scholz, J. Schneider-Mergener, and W. Honhe. 1997. Crystallographic analysis of anti-p24 (HIV-I) monoclonal antibody cross-reactivity and polyspecificity. Cell. 91:811-820.
    • (1997) Cell , vol.91 , pp. 811-820
    • Keitel, T.1    Kramer, A.2    Wessner, H.3    Scholz, C.4    Schneider-Mergener, J.5    Honhe, W.6
  • 16
    • 0029844217 scopus 로고    scopus 로고
    • A structure of the complex between concanavalin A and methyl-3,6-di-O-(α-D-mannopyranosyl)-α-D-mannopyranoside reveals two binding modes
    • Loris, R., D. Maes, F. Poortmans, L. Wyns, and J. Bouckaert. 1996. A structure of the complex between concanavalin A and methyl-3,6-di-O-(α-D-mannopyranosyl)-α-D-mannopyranoside reveals two binding modes. J. Biol. Chem. 271:30614-30618.
    • (1996) J. Biol. Chem. , vol.271 , pp. 30614-30618
    • Loris, R.1    Maes, D.2    Poortmans, F.3    Wyns, L.4    Bouckaert, J.5
  • 17
    • 0032560570 scopus 로고    scopus 로고
    • Two binding modes reveal flexibility in kinase/response regulator interactions in the bacterial chemotaxis pathway
    • McEvoy, M., A. C. Hausrath, G. B. Randolph, and S. J. Remington. 1998. Two binding modes reveal flexibility in kinase/response regulator interactions in the bacterial chemotaxis pathway Proc. Natl. Acad. Sci. U.S.A. 95:7333-7338.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 7333-7338
    • McEvoy, M.1    Hausrath, A.C.2    Randolph, G.B.3    Remington, S.J.4
  • 18
    • 0032586737 scopus 로고    scopus 로고
    • Man alpha1→2 Man alpha-OMe-concanavalin A complex reveals a balance of forces involved in carbohydrate recognition
    • Moothoo, D. N., B. Canan, R. A. Field, and J. H. Naismith. 1999. Man alpha1→2 Man alpha-OMe-concanavalin A complex reveals a balance of forces involved in carbohydrate recognition. Glycobiology. 9:539-545.
    • (1999) Glycobiology , vol.9 , pp. 539-545
    • Moothoo, D.N.1    Canan, B.2    Field, R.A.3    Naismith, J.H.4
  • 19
    • 0029067489 scopus 로고
    • Specificity of ligand binding in a buried nonpolar cavity of T4 lysozyme: Linkage of dynamics and structural plasticity
    • Morton, A., and B. W. Matthews. 1995. Specificity of ligand binding in a buried nonpolar cavity of T4 lysozyme: linkage of dynamics and structural plasticity. Biochemistry. 34:8576-8588.
    • (1995) Biochemistry , vol.34 , pp. 8576-8588
    • Morton, A.1    Matthews, B.W.2
  • 20
    • 0033551685 scopus 로고    scopus 로고
    • Structure-function analysis of tritrypticin, an antibacterial peptide of innate immune origin
    • Nagpal, S., V. Gupta, K. J. Kaur, and D. M. Salunke. 1999. Structure-function analysis of tritrypticin, an antibacterial peptide of innate immune origin. J. Biol. Chem. 274:23296-23304.
    • (1999) J. Biol. Chem. , vol.274 , pp. 23296-23304
    • Nagpal, S.1    Gupta, V.2    Kaur, K.J.3    Salunke, D.M.4
  • 21
    • 0028038824 scopus 로고
    • Refined structure of concanavalin A complexed with methyl D-mannopyranoside at 2.0 Å resolution and comparison with the saccharide-free structure
    • Naismith, J. H., C. Emmerich, J. Habash, S. J. Harrop, J. R. Helliwell, W. N. Hunter, J. Raftery, A. J. Kalb (Gilboa), and J. Yariv. 1994. Refined structure of concanavalin A complexed with methyl D-mannopyranoside at 2.0 Å resolution and comparison with the saccharide-free structure Acta Crystallogr. D50:847-858.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 847-858
    • Naismith, J.H.1    Emmerich, C.2    Habash, J.3    Harrop, S.J.4    Helliwell, J.R.5    Hunter, W.N.6    Raftery, J.7    Kalb, A.J.8    Yariv, J.9
  • 22
    • 0030042401 scopus 로고    scopus 로고
    • Structural basis of trimannoside recognition by concanavalin A
    • Naismith, J. H., and R. A. Field. 1996. Structural basis of trimannoside recognition by concanavalin A. J. Biol. Chem. 271:972-976.
    • (1996) J. Biol. Chem. , vol.271 , pp. 972-976
    • Naismith, J.H.1    Field, R.A.2
  • 23
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza, J. 1994. AMoRe: an automated package for molecular replacement. Acta Crystallogr. A50:157-163.
    • (1994) Acta Crystallogr. , vol.A50 , pp. 157-163
    • Navaza, J.1
  • 25
    • 0002452464 scopus 로고
    • Oscillation data reduction program
    • Sawyer, L., Isaasc, N., and Bailey, S., editors., SERC Daresbury Laboratory, Warrington, UK
    • Otwinowski, Z. 1993. Oscillation data reduction program. In Proceedings of the CCP4 Study Weekend: Data collection and Processing. Sawyer, L., Isaasc, N., and Bailey, S., editors., SERC Daresbury Laboratory, Warrington, UK, 56-62.
    • (1993) Proceedings of the CCP4 Study Weekend: Data Collection and Processing , pp. 56-62
    • Otwinowski, Z.1
  • 26
    • 0034705343 scopus 로고    scopus 로고
    • Aspartyl tRNA-synthetase from Escherichia coli: Flexibility and adaptability to the substrates
    • Rees, B., G. Webster, M. Delarue, M. Boeglin, and D. Moras. 2000. Aspartyl tRNA-synthetase from Escherichia coli: flexibility and adaptability to the substrates. J. Mol. Biol. 299:1157-1164.
    • (2000) J. Mol. Biol. , vol.299 , pp. 1157-1164
    • Rees, B.1    Webster, G.2    Delarue, M.3    Boeglin, M.4    Moras, D.5
  • 28
    • 0032811591 scopus 로고    scopus 로고
    • Crystallographic and calorimetric analysis of peptide binding to OppA protein
    • Sleigh, S. H., P. R. Seavers, A. J. Wilkinson, J. E. Ladbury, and J. R. Tame. 1999. Crystallographic and calorimetric analysis of peptide binding to OppA protein. J. Mol. Biol. 291:393-415.
    • (1999) J. Mol. Biol. , vol.291 , pp. 393-415
    • Sleigh, S.H.1    Seavers, P.R.2    Wilkinson, A.J.3    Ladbury, J.E.4    Tame, J.R.5
  • 29
    • 0033080945 scopus 로고    scopus 로고
    • Dual conformations for the HIV-1 gp120 V3 loop in complexes with different neutralizing Fabs
    • Stanfield, R. L., E. Cabezas, A. C. Satterthwait, E. A. Stura, A. T. Pfy, and I. A. Wilson. 1999. Dual conformations for the HIV-1 gp120 V3 loop in complexes with different neutralizing Fabs. Structure. 7:131-142.
    • (1999) Structure , vol.7 , pp. 131-142
    • Stanfield, R.L.1    Cabezas, E.2    Satterthwait, A.C.3    Stura, E.A.4    Pfy, A.T.5    Wilson, I.A.6
  • 30
    • 0034660904 scopus 로고    scopus 로고
    • Luxury accommodations: The expanding role of structural plasticity in protein-protein interactions
    • Sundberg, E. J., and R. A. Mariuzza. 2000. Luxury accommodations: the expanding role of structural plasticity in protein-protein interactions. Structure. 8:R137-R142.
    • (2000) Structure , vol.8
    • Sundberg, E.J.1    Mariuzza, R.A.2
  • 31
    • 0026481991 scopus 로고
    • High plasticity of multi-specific DNA methyltransferases in the region carrying DNA target recognizing enzyme modules
    • Trautner, W. J., and M. Noyer-Weidner. 1992. High plasticity of multi-specific DNA methyltransferases in the region carrying DNA target recognizing enzyme modules. EMBO J. 11:4445-4450.
    • (1992) EMBO J. , vol.11 , pp. 4445-4450
    • Trautner, W.J.1    Noyer-Weidner, M.2
  • 32
    • 0032783793 scopus 로고    scopus 로고
    • The structure, organization, activation and plasticity of the erythropoietin receptor
    • Wilson, I. A., and L. K. Jolliffe. 1999. The structure, organization, activation and plasticity of the erythropoietin receptor Curr. Opin. Struct. Biol. 9:696-704.
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 696-704
    • Wilson, I.A.1    Jolliffe, L.K.2


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