메뉴 건너뛰기




Volumn 372, Issue 2, 2007, Pages 549-561

Molecular Principles of the Interactions of Disordered Proteins

Author keywords

disorder to order transition; intrinsically unstructured proteins; molecular recognition; protein protein interactions; protein protein interface

Indexed keywords

ACTIN; AMINO ACID; BETA CATENIN; CALCIUM BINDING PROTEIN; CYCLINE; DNA BINDING PROTEIN; FIBRONECTIN; GLOBULAR PROTEIN; GUANOSINE TRIPHOSPHATASE; HYDROLASE; INITIATION FACTOR 4E; ISOMERASE; MEMBRANE PROTEIN; MYELIN BASIC PROTEIN; NEUROTOXIN; OXIDOREDUCTASE; PHOSPHOTRANSFERASE; PROTEIN C MYB; PROTEIN CDC42; PROTEIN P53; PROTEIN TYROSINE KINASE; RNA POLYMERASE; SERINE PROTEINASE INHIBITOR; SMAD2 PROTEIN; SNARE PROTEIN; TRANSFERASE; TROPONIN C; TROPONIN I; UNINDEXED DRUG; UVOMORULIN;

EID: 34547943482     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.07.004     Document Type: Article
Times cited : (238)

References (55)
  • 1
    • 5044235050 scopus 로고    scopus 로고
    • Ten thousand interactions for the molecular biologist
    • Aloy P., and Russell R.B. Ten thousand interactions for the molecular biologist. Nature Biotechnol. 22 (2004) 1317-1321
    • (2004) Nature Biotechnol. , vol.22 , pp. 1317-1321
    • Aloy, P.1    Russell, R.B.2
  • 2
    • 33644550021 scopus 로고    scopus 로고
    • Structural systems biology: modelling protein interactions
    • Aloy P., and Russell R.B. Structural systems biology: modelling protein interactions. Nature Rev. Mol. Cell Biol. 7 (2006) 188-197
    • (2006) Nature Rev. Mol. Cell Biol. , vol.7 , pp. 188-197
    • Aloy, P.1    Russell, R.B.2
  • 3
    • 33644555054 scopus 로고    scopus 로고
    • Proteome survey reveals modularity of the yeast cell machinery
    • Gavin A.C., Aloy P., Grandi P., Krause R., Boesche M., Marzioch M., et al. Proteome survey reveals modularity of the yeast cell machinery. Nature 440 (2006) 631-636
    • (2006) Nature , vol.440 , pp. 631-636
    • Gavin, A.C.1    Aloy, P.2    Grandi, P.3    Krause, R.4    Boesche, M.5    Marzioch, M.6
  • 4
    • 33745160404 scopus 로고    scopus 로고
    • Large-scale identification of protein-protein interaction of Escherichia coli K-12
    • Arifuzzaman M., Maeda M., Itoh A., Nishikata K., Takita C., Saito R., et al. Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res. 16 (2006) 686-691
    • (2006) Genome Res. , vol.16 , pp. 686-691
    • Arifuzzaman, M.1    Maeda, M.2    Itoh, A.3    Nishikata, K.4    Takita, C.5    Saito, R.6
  • 5
    • 0030028728 scopus 로고    scopus 로고
    • Principles of protein-protein interactions
    • Jones S., and Thornton J.M. Principles of protein-protein interactions. Proc. Natl Acad. Sci. USA 93 (1996) 13-20
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 13-20
    • Jones, S.1    Thornton, J.M.2
  • 6
    • 0003187567 scopus 로고    scopus 로고
    • The atomic structure of protein-protein recognition sites
    • Lo Conte L., Chothia C., and Janin J. The atomic structure of protein-protein recognition sites. J. Mol. Biol. 285 (1999) 2177-2198
    • (1999) J. Mol. Biol. , vol.285 , pp. 2177-2198
    • Lo Conte, L.1    Chothia, C.2    Janin, J.3
  • 7
    • 0041312697 scopus 로고    scopus 로고
    • Diversity of protein-protein interactions
    • Nooren I.M., and Thornton J.M. Diversity of protein-protein interactions. EMBO J. 22 (2003) 3486-3492
    • (2003) EMBO J. , vol.22 , pp. 3486-3492
    • Nooren, I.M.1    Thornton, J.M.2
  • 8
    • 11844249426 scopus 로고    scopus 로고
    • Hot regions in protein-protein interactions: the organization and contribution of structurally conserved hot spot residues
    • Keskin O., Ma B., and Nussinov R. Hot regions in protein-protein interactions: the organization and contribution of structurally conserved hot spot residues. J. Mol. Biol. 345 (2005) 1281-1294
    • (2005) J. Mol. Biol. , vol.345 , pp. 1281-1294
    • Keskin, O.1    Ma, B.2    Nussinov, R.3
  • 10
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm
    • Wright P.E., and Dyson H.J. Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm. J. Mol. Biol. 293 (1999) 321-331
    • (1999) J. Mol. Biol. , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 11
    • 0034669882 scopus 로고    scopus 로고
    • Why are "natively unfolded" proteins unstructured under physiologic conditions?
    • Uversky V.N., Gillespie J.R., and Fink A.L. Why are "natively unfolded" proteins unstructured under physiologic conditions?. Proteins: Struct. Funct. Genet. 41 (2000) 415-427
    • (2000) Proteins: Struct. Funct. Genet. , vol.41 , pp. 415-427
    • Uversky, V.N.1    Gillespie, J.R.2    Fink, A.L.3
  • 12
    • 0036408751 scopus 로고    scopus 로고
    • Intrinsic disorder in cell-signaling and cancer-associated proteins
    • Iakoucheva L., Brown C., Lawson J., Obradovic Z., and Dunker A. Intrinsic disorder in cell-signaling and cancer-associated proteins. J. Mol. Biol. 323 (2002) 573-584
    • (2002) J. Mol. Biol. , vol.323 , pp. 573-584
    • Iakoucheva, L.1    Brown, C.2    Lawson, J.3    Obradovic, Z.4    Dunker, A.5
  • 14
    • 25144472591 scopus 로고    scopus 로고
    • Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling
    • Uversky V.N., Oldfield C.J., and Dunker A.K. Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling. J. Mol. Recognit. 18 (2005) 343-384
    • (2005) J. Mol. Recognit. , vol.18 , pp. 343-384
    • Uversky, V.N.1    Oldfield, C.J.2    Dunker, A.K.3
  • 15
    • 1542358787 scopus 로고    scopus 로고
    • Prediction and functional analysis of native disorder in proteins from the three kingdoms of life
    • Ward J.J., Sodhi J.S., McGuffin L.J., Buxton B.F., and Jones D.T. Prediction and functional analysis of native disorder in proteins from the three kingdoms of life. J. Mol. Biol. 337 (2004) 635-645
    • (2004) J. Mol. Biol. , vol.337 , pp. 635-645
    • Ward, J.J.1    Sodhi, J.S.2    McGuffin, L.J.3    Buxton, B.F.4    Jones, D.T.5
  • 16
    • 33747191719 scopus 로고    scopus 로고
    • Prevalent structural disorder in E. coli and S. cerevisiae proteomes
    • Tompa P., Dosztányi Z., and Simon I. Prevalent structural disorder in E. coli and S. cerevisiae proteomes. J. Proteome Res. 5 (2006) 1996-2000
    • (2006) J. Proteome Res. , vol.5 , pp. 1996-2000
    • Tompa, P.1    Dosztányi, Z.2    Simon, I.3
  • 17
    • 3442902456 scopus 로고    scopus 로고
    • The role of structural disorder in the function of RNA and protein chaperones
    • Tompa P., and Csermely P. The role of structural disorder in the function of RNA and protein chaperones. FASEB J. 18 (2004) 1169-1175
    • (2004) FASEB J. , vol.18 , pp. 1169-1175
    • Tompa, P.1    Csermely, P.2
  • 18
    • 0036468397 scopus 로고    scopus 로고
    • Coupling of folding and binding for unstructured proteins
    • Dyson H.J., and Wright P.E. Coupling of folding and binding for unstructured proteins. Curr. Opin. Struct. Biol. 12 (2002) 54-60
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 54-60
    • Dyson, H.J.1    Wright, P.E.2
  • 19
    • 2542492280 scopus 로고    scopus 로고
    • Coupling of folding and binding of thymosin β4 upon interaction with monomeric actin monitored by nuclear magnetic resonance
    • Domanski M., Hertzog M., Coutant J., Gutsche-Perelroizen I., Bontems F., Carlier M.F., et al. Coupling of folding and binding of thymosin β4 upon interaction with monomeric actin monitored by nuclear magnetic resonance. J. Biol. Chem. 279 (2004) 23637-23645
    • (2004) J. Biol. Chem. , vol.279 , pp. 23637-23645
    • Domanski, M.1    Hertzog, M.2    Coutant, J.3    Gutsche-Perelroizen, I.4    Bontems, F.5    Carlier, M.F.6
  • 20
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson H.J., and Wright P.E. Intrinsically unstructured proteins and their functions. Nature Rev. Mol. Cell Biol. 6 (2005) 197-208
    • (2005) Nature Rev. Mol. Cell Biol. , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 21
    • 20444376186 scopus 로고    scopus 로고
    • The interplay between structure and function in intrinsically unstructured proteins
    • Tompa P. The interplay between structure and function in intrinsically unstructured proteins. FEBS Letters 579 (2005) 3346-3354
    • (2005) FEBS Letters , vol.579 , pp. 3346-3354
    • Tompa, P.1
  • 22
    • 27144464910 scopus 로고    scopus 로고
    • Flexible nets. The roles of intrinsic disorder in protein interaction networks
    • Dunker A.K., Cortese M.S., Romero P., Iakoucheva L.M., and Uversky V.N. Flexible nets. The roles of intrinsic disorder in protein interaction networks. FEBS J. 272 (2005) 5129-5148
    • (2005) FEBS J. , vol.272 , pp. 5129-5148
    • Dunker, A.K.1    Cortese, M.S.2    Romero, P.3    Iakoucheva, L.M.4    Uversky, V.N.5
  • 24
    • 33645214608 scopus 로고    scopus 로고
    • Disordered domains and high surface charge confer hubs with the ability to interact with multiple proteins in interaction networks
    • Patil A., and Nakamura H. Disordered domains and high surface charge confer hubs with the ability to interact with multiple proteins in interaction networks. FEBS Letters 580 (2006) 2041-2045
    • (2006) FEBS Letters , vol.580 , pp. 2041-2045
    • Patil, A.1    Nakamura, H.2
  • 25
    • 33750999318 scopus 로고    scopus 로고
    • Disorder and sequence repeats in hub proteins and their implications for network evolution
    • Dosztányi Z., Chen J., Dunker A.K., Simon I., and Tompa P. Disorder and sequence repeats in hub proteins and their implications for network evolution. J. Proteome Res. 5 (2006) 2985-2995
    • (2006) J. Proteome Res. , vol.5 , pp. 2985-2995
    • Dosztányi, Z.1    Chen, J.2    Dunker, A.K.3    Simon, I.4    Tompa, P.5
  • 26
    • 14844361449 scopus 로고    scopus 로고
    • Primary contact sites in intrinsically unstructured proteins: the case of calpastatin and microtubule-associated protein 2
    • Csizmok V., Bokor M., Banki P., Klement É., Medzihradszky K.F., Friedrich P., et al. Primary contact sites in intrinsically unstructured proteins: the case of calpastatin and microtubule-associated protein 2. Biochemistry 44 (2005) 3955-3964
    • (2005) Biochemistry , vol.44 , pp. 3955-3964
    • Csizmok, V.1    Bokor, M.2    Banki, P.3    Klement, É.4    Medzihradszky, K.F.5    Friedrich, P.6
  • 27
    • 2142757231 scopus 로고    scopus 로고
    • Preformed structural elements feature in partner recognition by intrinsically unstructured proteins
    • Fuxreiter M., Simon I., Friedrich P., and Tompa P. Preformed structural elements feature in partner recognition by intrinsically unstructured proteins. J. Mol. Biol. 338 (2004) 1015-1026
    • (2004) J. Mol. Biol. , vol.338 , pp. 1015-1026
    • Fuxreiter, M.1    Simon, I.2    Friedrich, P.3    Tompa, P.4
  • 28
  • 30
    • 34249695447 scopus 로고    scopus 로고
    • Local structural disorder imparts plasticity on linear motifs
    • Fuxreiter M., Tompa P., and Simon I. Local structural disorder imparts plasticity on linear motifs. Bioinformatics 23 (2007) 950-956
    • (2007) Bioinformatics , vol.23 , pp. 950-956
    • Fuxreiter, M.1    Tompa, P.2    Simon, I.3
  • 31
    • 20444414545 scopus 로고    scopus 로고
    • Linear motifs: evolutionary interaction switches
    • Neduva V., and Russell R.B. Linear motifs: evolutionary interaction switches. FEBS Letters 579 (2005) 3342-3345
    • (2005) FEBS Letters , vol.579 , pp. 3342-3345
    • Neduva, V.1    Russell, R.B.2
  • 32
    • 4143107222 scopus 로고    scopus 로고
    • Analysis of ordered and disordered protein complexes reveals structural features discriminating between stable and unstable monomers
    • Gunasekaran K., Tsai C.J., and Nussinov R. Analysis of ordered and disordered protein complexes reveals structural features discriminating between stable and unstable monomers. J. Mol. Biol. 341 (2004) 1327-1341
    • (2004) J. Mol. Biol. , vol.341 , pp. 1327-1341
    • Gunasekaran, K.1    Tsai, C.J.2    Nussinov, R.3
  • 36
    • 0035805117 scopus 로고    scopus 로고
    • The structure of the β-catenin/E-cadherin complex and the molecular basis of diverse ligand recognition by β-catenin
    • Huber A.H., and Weis W.I. The structure of the β-catenin/E-cadherin complex and the molecular basis of diverse ligand recognition by β-catenin. Cell 105 (2001) 391-402
    • (2001) Cell , vol.105 , pp. 391-402
    • Huber, A.H.1    Weis, W.I.2
  • 37
    • 2542421811 scopus 로고    scopus 로고
    • The β-thymosin/WH2 domain; structural basis for the switch from inhibition to promotion of actin assembly
    • Hertzog M., van Heijenoort C., Didry D., Gaudier M., Coutant J., Gigant B., et al. The β-thymosin/WH2 domain; structural basis for the switch from inhibition to promotion of actin assembly. Cell 117 (2004) 611-623
    • (2004) Cell , vol.117 , pp. 611-623
    • Hertzog, M.1    van Heijenoort, C.2    Didry, D.3    Gaudier, M.4    Coutant, J.5    Gigant, B.6
  • 38
    • 1842766125 scopus 로고    scopus 로고
    • 28/FlgM reveals an intact sigma factor in an inactive conformation
    • 28/FlgM reveals an intact sigma factor in an inactive conformation. Mol. Cell 14 (2004) 127-138
    • (2004) Mol. Cell , vol.14 , pp. 127-138
    • Sorenson, M.K.1    Ray, S.S.2    Darst, S.A.3
  • 39
    • 14844342815 scopus 로고    scopus 로고
    • The pairwise energy content estimated from amino acid composition discriminates between folded and intrinsically unstructured proteins
    • Dosztányi Z., Csizmok V., Tompa P., and Simon I. The pairwise energy content estimated from amino acid composition discriminates between folded and intrinsically unstructured proteins. J. Mol. Biol. 347 (2005) 827-839
    • (2005) J. Mol. Biol. , vol.347 , pp. 827-839
    • Dosztányi, Z.1    Csizmok, V.2    Tompa, P.3    Simon, I.4
  • 40
    • 24044538903 scopus 로고    scopus 로고
    • IUPred: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content
    • Dosztányi Z., Csizmok V., Tompa P., and Simon I. IUPred: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content. Bioinformatics 21 (2005) 3433-3434
    • (2005) Bioinformatics , vol.21 , pp. 3433-3434
    • Dosztányi, Z.1    Csizmok, V.2    Tompa, P.3    Simon, I.4
  • 41
    • 0036803243 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins
    • Tompa P. Intrinsically unstructured proteins. Trends Biochem. Sci. 27 (2002) 527-533
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 527-533
    • Tompa, P.1
  • 43
    • 0030768266 scopus 로고    scopus 로고
    • Structural motifs at protein-protein interfaces: protein cores versus two-state and three-state model complexes
    • Tsai C.J., Xu D., and Nussinov R. Structural motifs at protein-protein interfaces: protein cores versus two-state and three-state model complexes. Protein. Sci. 6 (1997) 1793-1805
    • (1997) Protein. Sci. , vol.6 , pp. 1793-1805
    • Tsai, C.J.1    Xu, D.2    Nussinov, R.3
  • 46
    • 33748280715 scopus 로고    scopus 로고
    • Abundance of intrinsic disorder in protein associated with cardiovascular disease
    • Cheng Y., LeGall T., Oldfield C.J., Dunker A.K., and Uversky V.N. Abundance of intrinsic disorder in protein associated with cardiovascular disease. Biochemistry 45 (2006) 10448-10460
    • (2006) Biochemistry , vol.45 , pp. 10448-10460
    • Cheng, Y.1    LeGall, T.2    Oldfield, C.J.3    Dunker, A.K.4    Uversky, V.N.5
  • 48
    • 10744221485 scopus 로고    scopus 로고
    • In vivo activation of the p53 pathway by small-molecule antagonists of MDM2
    • Vassilev L.T., Vu B.T., Graves B., Carvajal D., Podlaski F., Filipovic Z., et al. In vivo activation of the p53 pathway by small-molecule antagonists of MDM2. Science 303 (2004) 844-848
    • (2004) Science , vol.303 , pp. 844-848
    • Vassilev, L.T.1    Vu, B.T.2    Graves, B.3    Carvajal, D.4    Podlaski, F.5    Filipovic, Z.6
  • 49
    • 0015222647 scopus 로고
    • The interpretation of protein structures: estimation of static accessibility
    • Lee B., and Richards F.M. The interpretation of protein structures: estimation of static accessibility. J. Mol. Biol. 55 (1971) 379-400
    • (1971) J. Mol. Biol. , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 50
    • 0000484499 scopus 로고
    • Hydrophobic parameters pi of amino-acid side chains from the partitioning of N-acetyl-amino-acid amides
    • Fauchere J.L., and Pliska V. Hydrophobic parameters pi of amino-acid side chains from the partitioning of N-acetyl-amino-acid amides. Eur. J. Med. Chem. 18 (1983) 369-375
    • (1983) Eur. J. Med. Chem. , vol.18 , pp. 369-375
    • Fauchere, J.L.1    Pliska, V.2
  • 51
    • 0029909384 scopus 로고    scopus 로고
    • An iterative method for extracting energy-like quantities from protein structures
    • Thomas P.D., and Dill K.A. An iterative method for extracting energy-like quantities from protein structures. Proc. Natl Acad. Sci. USA 93 (1996) 11628-11633
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 11628-11633
    • Thomas, P.D.1    Dill, K.A.2
  • 52
    • 34347388470 scopus 로고    scopus 로고
    • UniRef: comprehensive and non-redundant UniProt reference clusters
    • Suzek B.E., Huang H., McGarvey P., Mazumder R., and Wu H.C. UniRef: comprehensive and non-redundant UniProt reference clusters. Bioinformatics 23 (2007) 1282-1288
    • (2007) Bioinformatics , vol.23 , pp. 1282-1288
    • Suzek, B.E.1    Huang, H.2    McGarvey, P.3    Mazumder, R.4    Wu, H.C.5
  • 53
    • 0035178383 scopus 로고    scopus 로고
    • Protein-protein interfaces: analysis of amino acid conservation in homodimers
    • Valdar W.S., and Thornton J.M. Protein-protein interfaces: analysis of amino acid conservation in homodimers. Proteins: Struct. Funct. Genet. 42 (2001) 108-124
    • (2001) Proteins: Struct. Funct. Genet. , vol.42 , pp. 108-124
    • Valdar, W.S.1    Thornton, J.M.2
  • 54
    • 0035878724 scopus 로고    scopus 로고
    • Improving the accuracy of PSI-BLAST protein database searches with composition-based statistics and other refinements
    • Schaffer A.A., Aravind L., Madden T.L., Shavirin S., Spouge J.L., Wolf Y.I., et al. Improving the accuracy of PSI-BLAST protein database searches with composition-based statistics and other refinements. Nucl. Acids Res. 29 (2001) 2994-3005
    • (2001) Nucl. Acids Res. , vol.29 , pp. 2994-3005
    • Schaffer, A.A.1    Aravind, L.2    Madden, T.L.3    Shavirin, S.4    Spouge, J.L.5    Wolf, Y.I.6
  • 55
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., and Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucl. Acids. Res. 22 (1994) 4673-4680
    • (1994) Nucl. Acids. Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.