메뉴 건너뛰기




Volumn 58, Issue 2, 2006, Pages 107-109

According to current textbooks, a well-defined three-dimensional structure is a prerequisite for the function of a protein. Is this correct?

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN BINDING PROTEIN; NUCLEIC ACID BINDING PROTEIN; RNA;

EID: 33646256176     PISSN: 15216543     EISSN: 15216551     Source Type: Journal    
DOI: 10.1080/15216540500484376     Document Type: Short Survey
Times cited : (18)

References (35)
  • 1
    • 0016709043 scopus 로고
    • X-ray analysis of glucagon and its relationship to receptor binding
    • Sasaki, K., Dockerill, S., Adamiak, D. A., Tickle, I. J., and Blundell, T. (1975) X-ray analysis of glucagon and its relationship to receptor binding. Nature 257, 751-757.
    • (1975) Nature , vol.257 , pp. 751-757
    • Sasaki, K.1    Dockerill, S.2    Adamiak, D.A.3    Tickle, I.J.4    Blundell, T.5
  • 2
    • 0018196016 scopus 로고
    • 1H nuclear-magnetic-resonance studies of the molecular conformation of monomeric glucagon in aqueous solution
    • 1H nuclear-magnetic-resonance studies of the molecular conformation of monomeric glucagon in aqueous solution. Eur. J. Biochem. 91, 209-214.
    • (1978) Eur. J. Biochem. , vol.91 , pp. 209-214
    • Boesch, C.1    Bundi, A.2    Oppliger, M.3    Wüthrich, K.4
  • 3
    • 0018184483 scopus 로고
    • The character of the stored molecules in chromaffin granules of the adrenal medulla: A nuclear magnetic resonance study
    • Daniels, A. J., Williams, R. J. P., and Wright, P. E. (1978) The character of the stored molecules in chromaffin granules of the adrenal medulla: a nuclear magnetic resonance study. Neuroscience 3, 573-585.
    • (1978) Neuroscience , vol.3 , pp. 573-585
    • Daniels, A.J.1    Williams, R.J.P.2    Wright, P.E.3
  • 6
    • 0036128797 scopus 로고    scopus 로고
    • Natively unfolded proteins: A point where biology waits for physics
    • Uversky, V. N. (2002) Natively unfolded proteins: a point where biology waits for physics. Protein Sci. 11, 739-756.
    • (2002) Protein Sci. , vol.11 , pp. 739-756
    • Uversky, V.N.1
  • 7
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: Re-assessing the protein structure-function paradigm
    • Wright, P. E., and Dyson, H. J. (1999) Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm. J. Mol. Biol. 293, 321-331.
    • (1999) J. Mol. Biol. , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 10
    • 0036803243 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins
    • Tompa, P. (2002) Intrinsically unstructured proteins. Trends Biochem. Sci. 27, 527.
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 527
    • Tompa, P.1
  • 11
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson, H. J., and Wright, P. E. (2005) Intrinsically unstructured proteins and their functions. Nat. Rev. Mol. Cell Biol. 6, 197-208.
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 12
    • 0034912536 scopus 로고    scopus 로고
    • Nuclear magnetic resonance methods for elucidation of structure and dynamics of disordered states
    • Dyson, H. J., and Wright, P. E. (2001) Nuclear magnetic resonance methods for elucidation of structure and dynamics of disordered states. Methods Enzymol. 339, 258-270.
    • (2001) Methods Enzymol. , vol.339 , pp. 258-270
    • Dyson, H.J.1    Wright, P.E.2
  • 13
    • 4344707281 scopus 로고    scopus 로고
    • Unfolded proteins and protein folding studied by NMR
    • Dyson, H. J., and Wright, P. E. (2004) Unfolded proteins and protein folding studied by NMR. Chem. Rev. 104, 3607-3622.
    • (2004) Chem. Rev. , vol.104 , pp. 3607-3622
    • Dyson, H.J.1    Wright, P.E.2
  • 14
    • 1342290303 scopus 로고    scopus 로고
    • Unfolded Proteins
    • Academic Press, San Diego
    • Rose, G. D. (2002). Unfolded Proteins. Advances in Protein Chemistry, 62. Academic Press, San Diego.
    • (2002) Advances in Protein Chemistry , pp. 62
    • Rose, G.D.1
  • 16
    • 0024403543 scopus 로고
    • The Q-linker: A class of interdomain sequences found in bacterial multidomain regulatory proteins
    • Wootton, J. C., and Drummond, M. H. (1989) The Q-linker: a class of interdomain sequences found in bacterial multidomain regulatory proteins. Protein Eng. Design Select. 2, 535-543.
    • (1989) Protein Eng. Design Select. , vol.2 , pp. 535-543
    • Wootton, J.C.1    Drummond, M.H.2
  • 17
    • 0037540052 scopus 로고    scopus 로고
    • Quantitative account of the enhanced affinity of two linked scFvs specific for different epitopes on the same antigen
    • Zhou, H. X. (2003) Quantitative account of the enhanced affinity of two linked scFvs specific for different epitopes on the same antigen. J. Mol. Biol. 329, 1-8.
    • (2003) J. Mol. Biol. , vol.329 , pp. 1-8
    • Zhou, H.X.1
  • 19
    • 0036468397 scopus 로고    scopus 로고
    • Coupling of folding and binding for unstructured proteins
    • Dyson, H. J., and Wright, P. E. (2002) Coupling of folding and binding for unstructured proteins. Curr. Opin. Struct. Biol. 12, 54-60.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 54-60
    • Dyson, H.J.1    Wright, P.E.2
  • 20
    • 0035096292 scopus 로고    scopus 로고
    • Recognition between flexible protein molecules: Induced and assisted folding
    • Demchenko, A. P. (2001) Recognition between flexible protein molecules: induced and assisted folding. J. Mol. Recogn. 14, 42-61.
    • (2001) J. Mol. Recogn. , vol.14 , pp. 42-61
    • Demchenko, A.P.1
  • 22
    • 0029993105 scopus 로고    scopus 로고
    • Analysis of the structural properties of cAMP-responsive element-binding protein (CREB) and phosphorylated CREB
    • Richards, J. P., Bächinger, H. P., Goodman, R. H., and Brennan, R. G. (1996) Analysis of the structural properties of cAMP-responsive element-binding protein (CREB) and phosphorylated CREB. J. Biol. Chem. 271, 13716-13723.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13716-13723
    • Richards, J.P.1    Bächinger, H.P.2    Goodman, R.H.3    Brennan, R.G.4
  • 23
    • 0344936739 scopus 로고    scopus 로고
    • Solution structure of the KIX domain of CBP bound to the transactivation domain of CREB: A model for activator:coactivator interactions
    • Radhakrishnan, I., Pérez-Alvarado, G. C., Parker, D., Dyson, H. J., Montminy, M. R., and Wright, P. E. (1997) Solution structure of the KIX domain of CBP bound to the transactivation domain of CREB: a model for activator:coactivator interactions. Cell 91, 741-752.
    • (1997) Cell , vol.91 , pp. 741-752
    • Radhakrishnan, I.1    Pérez-Alvarado, G.C.2    Parker, D.3    Dyson, H.J.4    Montminy, M.R.5    Wright, P.E.6
  • 24
    • 0035932969 scopus 로고    scopus 로고
    • Solution structure of DFF40 and DFF45 N-terminal domain complex and mutual chaperone activity of DFF40 and DFF45
    • Zhou, P., Lugovskoy, A. A., McCarty, J. S., Li, P., and Wagner, G. (2001) Solution structure of DFF40 and DFF45 N-terminal domain complex and mutual chaperone activity of DFF40 and DFF45. PNAS 98, 6051-6055.
    • (2001) PNAS , vol.98 , pp. 6051-6055
    • Zhou, P.1    Lugovskoy, A.A.2    McCarty, J.S.3    Li, P.4    Wagner, G.5
  • 27
    • 0038392752 scopus 로고    scopus 로고
    • Structural basis for negative regulation of hypoxia-inducible factor-1alpha by CITED2
    • Freedman, S. J., Sun, Z. Y., Kung, A. L., France, D. S., Wagner, G., and Eck, M. J. (2003) Structural basis for negative regulation of hypoxia-inducible factor-1alpha by CITED2. Nat. Struct. Biol. 10, 504-512.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 504-512
    • Freedman, S.J.1    Sun, Z.Y.2    Kung, A.L.3    France, D.S.4    Wagner, G.5    Eck, M.J.6
  • 28
    • 1642576027 scopus 로고    scopus 로고
    • Interaction of the TAZ1 domain of CREB-binding protein with the activation domain of CITED2: Regulation by competition between intrinsically unstructured ligands for non-identical binding sites
    • De Guzman, R. N., Martinez-Yamout, M., Dyson, H. J., and Wright, P. E. (2004) Interaction of the TAZ1 domain of CREB-binding protein with the activation domain of CITED2: regulation by competition between intrinsically unstructured ligands for non-identical binding sites. J. Biol. Chem. 279, 3042-3049.
    • (2004) J. Biol. Chem. , vol.279 , pp. 3042-3049
    • De Guzman, R.N.1    Martinez-Yamout, M.2    Dyson, H.J.3    Wright, P.E.4
  • 30
    • 0025017975 scopus 로고
    • Altered protein conformation on DNA binding by Fos and Jun
    • Patel, L., Abate, C., and Curran, T. (1990) Altered protein conformation on DNA binding by Fos and Jun. Nature 347, 572-574.
    • (1990) Nature , vol.347 , pp. 572-574
    • Patel, L.1    Abate, C.2    Curran, T.3
  • 31
    • 0037675852 scopus 로고    scopus 로고
    • Mutual induced fit binding of Xenopus ribosomal protein L5 to 5S rRNA
    • DiNitto, J. P., and Huber, P. W. (2003) Mutual induced fit binding of Xenopus ribosomal protein L5 to 5S rRNA. J. Mol. Biol. 330, 979-992.
    • (2003) J. Mol. Biol. , vol.330 , pp. 979-992
    • DiNitto, J.P.1    Huber, P.W.2
  • 34
    • 0034255123 scopus 로고    scopus 로고
    • Speeding molecular recognition by using the folding funnel: The fly-casting mechanism
    • Shoemaker, B. A., Portman, J. J., and Wolynes, P. G. (2000) Speeding molecular recognition by using the folding funnel: the fly-casting mechanism. Proc. Natl. Acad. Sci. USA 97, 8868-8873.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8868-8873
    • Shoemaker, B.A.1    Portman, J.J.2    Wolynes, P.G.3
  • 35
    • 0028947257 scopus 로고
    • Funnels, pathways, and the energy landscape of protein folding: A synthesis
    • Bryngelson, J. D., Onuchic, J. N., Socci, N. D., and Wolynes, P. G. (1995) Funnels, pathways, and the energy landscape of protein folding: a synthesis. Proteins 21, 167-195.
    • (1995) Proteins , vol.21 , pp. 167-195
    • Bryngelson, J.D.1    Onuchic, J.N.2    Socci, N.D.3    Wolynes, P.G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.