Functional anthology of intrinsic disorder. 1. Biological processes and functions of proteins with long disordered regions

Journal of Proteome Research

Volumn 6, Issue 5, 2007, Pages 1882-1898

  Xie, Hongbo ^a   Vucetic, Slobodan ^a   Iakoucheva, Lilia M ^b   Oldfield, Christopher J ^c   Dunker, A Keith ^c   Uversky, Vladimir N ^c,d   Obradovic, Zoran ^a  

^a TEMPLE UNIVERSITY   (United States)

^b ROCKEFELLER UNIVERSITY   (United States)

^c INDIANA UNIVERSITY   (United States)

^d INSTITUTE FOR BIOLOGICAL INSTRUMENTATION   (Russian Federation)

Author keywords

Bioinformatics; Disorder prediction; Intrinsic disorder; Intrinsically disordered proteins; Protein function; Protein structure

Indexed keywords

AMINO ACID SEQUENCE; ARTICLE; BIOINFORMATICS; MOLECULAR BIOLOGY; PREDICTION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DATABASE; PROTEIN FUNCTION; PROTEIN STRUCTURE; PROTEOMICS; SWISS-PROT;

ALGORITHMS; ANIMALS; COMPUTATIONAL BIOLOGY; DATABASES, PROTEIN; HUMANS; PROTEIN CONFORMATION; PROTEINS; SEQUENCE ANALYSIS, PROTEIN;

EID: 33847768609     PISSN: 15353893     EISSN: None     Source Type: Journal    
DOI: 10.1021/pr060392u     Document Type: Article

References (216)

1. Fischer, E. Einfluss der Configuration auf die Wirkung der Enzyme. Ber. Dtsch. Chem. Ges. 1894, 27, 2985-2993.
2. Wu, H. Studies on denaturation of proteins XIII - a theory of denaturation. Chin. J. Physiol. 1931, 1, 219-234.
3. Mirsky, A. E.; Pauling, L. On the structure of native, denatured, and coagulated proteins. Proc. Natl. Acad. Sci. U.S.A. 1936, 22, 439-447.
4. Sela, M.; White, F. H., Jr.; Anfinsen, C. B. Reductive cleavage of disulfide bridges in ribonuclease. Science 1957, 125, 691-692.
5. Berman, H. M.; Westbrook, J.; Feng, Z.; Gilliland, G.; Bhat, T. N.; Weissig, H.; Shindyalov, I. N.; Bourne, P. E. The Protein Data Bank. Nucleic Acids Res. 2000, 28, 235-242.
6. Dunker, A. K.; Lawson, J. D.; Brown, C. J.; Williams, R. M.; Romero, P.; Oh, J. S.; Oldfield, C. J.; Campen, A. M.; Ratliff, C. M.; Hipps, K. W.; Ausio, J.; Nissen, M. S.; Reeves, R.; Kang, C.; Kissinger, C. R.; Bailey, R. W.; Griswold, M. D.; Chiu, W.; Garner, E. C.; Obradovic, Z. Intrinsically disordered protein. J. Mol. Graphics Modell. 2001, 19, 26-59.
7. Uversky, V. N. Natively unfolded proteins: a point where biology waits for physics. Protein Sci. 2002, 11, 739-756.
8. Dunker, A. K.; Brown, C. J.; Lawson, J. D.; Iakoucheva, L. M.; Obradovic, Z. Intrinsic disorder and protein function. Biochemistry 2002, 41, 6573-6582.
9. Dunker, A. K.; Brown, C. J.; Obradovic, Z. Identification and functions of usefully disordered proteins. Adv. Protein Chem. 2002, 62, 25-49.
10. Tompa, P. Intrinsically unstructured proteins. Trends Biochem. Sci. 2002, 27, 527-533.
11. Wright, P. E.; Dyson, H. J. Intrinsically unstructured proteins: reassessing the protein structure-function paradigm. J. Mol. Biol. 1999, 293, 321-331.
12. Dunker, A. K.; Obradovic, Z. The protein trinity-linking function and disorder. Nat. Biotechnol. 2001, 19, 805-806.
13. Uversky, V. N. What does it mean to be natively unfolded? Eur. J. Biochem. 2002, 269, 2-12.
14. Oldfield, C. J.; Cheng, Y.; Cortese, M. S.; Brown, C. J.; Uversky, V. N.; Dunker, A. K. Comparing and combining predictors of mostly disordered proteins. Biochemistry 2005, 44, 1989-2000.
15. Dunker, A. K.; Obradovic, Z.; Romero, P.; Garner, E. C.; Brown, C. J. Intrinsic protein disorder in complete genomes. Genome Inf. Ser. 2000, 11, 161-171.
16. Iakoucheva, L. M.; Brown, C. J.; Lawson, J. D.; Obradovic, Z.; Dunker, A. K. Intrinsic disorder in cell-signaling and cancer-associated proteins. J. Mol. Biol. 2002, 323, 573-584.
17. Uversky, V. N.; Gillespie, J. R.; Fink, A. L. Why are "natively unfolded" proteins unstructured under physiologic conditions? Proteins 2000, 41, 415-427.
18. Dyson, H. J.; Wright, P. E. Coupling of folding and binding for unstructured proteins. Curr. Opin. Struct. Biol. 2002, 12, 54-60.
19. Dyson, H. J.; Wright, P. E. Intrinsically unstructured proteins and their functions. Nat. Rev. Mol. Cell Biol. 2005, 6, 197-208.
20. Daughdrill, G. W.; Pielak, G. J.; Uversky, V. N.; Cortese, M. S.; Dunker, A. K. Natively disordered proteins. In Handbook of Protein Folding; Buchner, J., Kiefhaber, T., Eds.; Wiley-VCH, Verlag GmbH & Co. KGaA: Weinheim, Germany, 2005; pp 271-353.
21. Dunker, A. K.; Cortese, M. S.; Romero, P.; Iakoucheva, L. M.; Uversky, V. N. Flexible nets. The roles of intrinsic disorder in protein interaction networks. FEBS J. 2005, 272, 5129-5148.
22. Uversky, V. N.; Oldfield, C. J.; Dunker, A. K. Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling. J. Mol. Recognit. 2005, 18, 343-384.
23. Haynes, C.; Oldfield, C. J.; Ji, F.; Klitgord, N.; Cusick, M. E.; Radivojac, P.; Uversky, V. N.; Vidal, M.; Iakoucheva, L. M. Intrinsic disorder is a common feature of hub proteins from four eukaryotic interactomes. PLoS Comput. Biol. 2006, 2, e100.
24. Vucetic, S.; Obradovic, Z.; Vacic, V.; Radivojac, P.; Peng, K.; Iakoucheva, L. M.; Cortese, M. S.; Lawson, J. D.; Brown, C. J.; Sikes, J. G.; Newton, C. D.; Dunker, A. K. DisProt: a database of protein disorder. Bioinformatics 2005, 21, 137-140.
25. Dyson, H. J.; Wright, P. E. According to current textbooks, a well-defined three-dimensional structure is a prerequisite for the function of a protein. Is this correct? IUBMB Life 2006, 58, 107-109.
26. Peng, K.; Vucetic, S.; Radivojac, P.; Brown, C. J.; Dunker, A. K.; Obradovic, Z. Optimizing long intrinsic disorder predictors with protein evolutionary information. J. Bioinf. Comput. Biol. 2005, 3, 35-60.
27. Boeckmann, B.; Bairoch, A.; Apweiler, R.; Blatter, M. C.; Estreicher, A.; Gasteiger, E.; Martin, M. J.; Michoud, K.; O'Donovan, C.; Phan, I.; Pilbout, S.; Schneider, M. The SWISS-PROT protein knowledgebase and its supplement TrEMBL in 2003. Nucleic Acids Res. 2003, 31, 365-370.
28. Ward, J. J.; Sodhi, J. S.; McGuffin, L. J.; Buxton, B. F.; Jones, D. T. Prediction and functional analysis of native disorder in proteins from the three kingdoms of life. J. Mol. Biol. 2004, 337, 635-645.
29. Xie, H.; Vucetic, S.; Iakoucheva, L. M.; Oldfield, C. J.; Dunker, A. K.; Obradovic, Z.; Uversky, V. N. Functional anthology of intrinsic disorder. 2. Cellular components, domains, technical terms, developmental processes, and coding sequence diversity associated with long disordered regions. J. Proteome Res. 2007, 5, 1899-1916.
30. Xie, H.; Vucetic, S.; Iakoucheva, L. M.; Oldfield, C. J.; Dunker, A. K.; Obradovic, Z.; Uversky, V. N. Functional anthology of intrinsic disorder. 3. Ligands, postranslational modifications, and diseases associated with long disordered regions. J. Proteome Res. 2007, 5, 1917-1932.
31. O'Donovan, C.; Martin, M. J.; Glemet, E.; Codani, J. J.; Apweiler, R. Removing redundancy in SWISS-PROT and TrEMBL. Bioinformatics 1999, 15, 258-259.
32. Enright, A. J.; Van, Dongen, S.; Ouzounis, C. A. An efficient algorithm for large-scale detection of protein families. Nucleic Acids Res. 2002, 30, 1575-1584.
33. Altschul, S. F.; Gish, W.; Miller, W.; Myers, E. W.; Lipman, D. J. Basic local alignment search tool. J. Mol. Biol. 1990, 215, 403-410.
34. Romero, P.; Obradovic, Z.; Dunker, A. K. Sequence data analysis for long disordered regions prediction in the calcineurin family. Genome Inf. Ser. 1997, 8, 110-124.
35. Romero, P.; Obradovic, Z.; Kissinger, C.; Villafranca, J. E.; Dunker, A. K. Identifying disordered regions in proteins from amino acid sequence. Proc. Int. Conf. Neural Networks 1997, 1, 90-95.
36. Xie, Q.; Arnold, G. E.; Romero, P.; Obradovic, Z.; Garner, E.; Dunker, A. K. The sequence attribute method for determining relationships between sequence and protein disorder. Genome Inf. Ser. 1998, 9, 193-200.
37. Romero, P.; Obradovic, Z.; Li, X.; Garner, E. C.; Brown, C. J.; Dunker, A. K. Sequence complexity of disordered protein. Proteins 2001, 42, 38-48.
38. Sickmeier, M.; Hamilton, J. A.; LeGall, T.; Vacic, V.; Cortese, M. S.; Tantos, A.; Szabo, B.; Tompa, P.; Chen, J.; Uversky, V. N.; Obradovic, Z.; Dunker, A. K. DisProt: the Database of Disordered Proteins. Nucleic Acids Res. 2007, 35, D786-793.
39. Blau, H. M.; Baltimore, D. Differentiation requires continuous regulation. J. Cell Biol. 1991, 112, 781-783.
40. Adams, J. C.; Watt, F. M. Regulation of development and differentiation by the extracellular matrix. Development 1993, 117, 1183-1198.
41. Watt, F. M. The extracellular matrix and cell shape. Trends Biochem. Sci. 1986, 11, 482-485.
42. Hay, E. D. Cell Biology of Extracellular Matrix; Plenum Press: New York, 1981.
43. Ruoslahti, E.; Pierschbacher, M. D. New perspectives in cell adhesion: RGD and integrins. Science 1987, 238, 491-497.
44. House-Pompeo, K.; Xu, Y.; Joh, D.; Speziale, P.; Hook, M. Conformational changes in the fibronectin binding MSCRAMMs are induced by ligand binding. J. Biol. Chem. 1996, 271, 1379-1384.
45. Kim, J. H.; Singvall, J.; Schwarz-Linek, U.; Johnson, B. J.; Potts, J. R.; Hook, M. BBK32, a fibronectin binding MSCRAMM from Borrelia burgdorferi, contains a disordered region that undergoes a conformational change on ligand binding. J. Biol. Chem. 2004, 279, 41706-41714.
46. Campbell, K. M.; Terrell, A. R.; Laybourn, P. J.; Lumb, K. J. Intrinsic structural disorder of the C-terminal activation domain from the bZIP transcription factor Fos. Biochemistry 2000, 39, 2708-2713.
47. Haynes, C.; Iakoucheva, L. M. Serine/arginine-rich splicing factors belong to a class of intrinsically disordered proteins. Nucleic Acids Res. 2006, 34, 305-312.
48. Bhalla, J.; Storchan, G. B.; Maccarthy, C. M.; Uversky, V. N.; Tcherkasskaya, O. Local flexibility in molecular function paradigm. Mol. Cell. Proteomics 2006, 5, 1212-1223.
49. Liu, J.; Perumal, N. B.; Oldfield, C. J.; Su, E. W.; Uversky, V. N.; Dunker, A. K. Intrinsic disorder in transcription factors. Biochemistry 2006, 45, 6873-6888.
50. Minezaki, Y.; Homma, K.; Kinjo, A. R.; Nishikawa, K. Human transcription factors contain a high fraction of intrinsically disordered regions essential for transcriptional regulation. J. Mol. Biol. 2006, 359, 1137-1149.
51. Lewis, J. D.; Abbott, D. W.; Ausio, J. A haploid affair: core histone transitions during spermatogenesis. Biochem. Cell Biol. 2003, 81, 131-140.
52. Ausio, J. Histone H1 and the evolution of the nuclear sperm-specific proteins. In Advances in Spermatozoal Phytogeny and Taxonomy, Jamieson, B. G. M., Ausio, J., Justine, J. L., Eds.; Memoires du Museum National d'Histoire Naturelle: Paris, France, 1995.
53. Ausio, J.; Subirana, J. A. A high molecular weight nuclear basic protein from the bivalve mollusc Spisula solidissima. J. Biol. Chem. 1982, 257, 2802-2805.
54. Ausio, J.; Toumadje, A.; McParland, R.; Becker, R. R.; Johnson, W. C. Jr.; van Holde, K. E. Structural characterization of the trypsin-resistant core in the nuclear sperm-specific protein from Spisula solidissima. Biochemistry 1987, 26, 975-982.
55. Lewis, J. D.; Ausio, J. Protamine-like proteins: evidence for a novel chromatin structure. Biochem. Cell Biol. 2002, 80, 353-361.
56. Lewis, J. D.; McParland, R.; Ausio, J. PL-I of Spisula solidissima, a highly elongated sperm-specific histone H1. Biochemistry 2004, 43, 7766-7775.
57. Harvey, A. C.; Downs, J. A. What functions do linker histones provide? Mol. Microbiol. 2004, 53, 771-775.
58. Isenberg, I. Histones. Annu. Rev. Biochem. 1979, 48, 159-191.
59. Boublik, M.; Bradbury, E. M.; Crane-Robinson, C. An investigation of the conformational changes in histones F1 and F2a1 by proton magnetic resonance spectroscopy. Eur. J. Biochem. 1970, 14, 486-497.
60. Li, H. J.; Wickett, R.; Craig, A. M.; Isenberg, I. Conformational changes in histone IV. Biopolymers 1972, 11, 375-397.
61. Wickett, R. R.; Li, H. J.; Isenberg, I. Salt effects on histone IV conformation. Biochemistry 1972, 11, 2952-2957.
62. D'Anna, J. A. Jr.; Isenberg, I. Conformational changes of histone ARE(F3, III). Biochemistry 1974, 13, 4987-4992.
63. D'Anna, J. A., Jr.; Isenberg, I. Conformational changes of histone LAK (f2a2). Biochemistry 1974, 13, 2093-2098.
64. Munishkina, L. A.; Fink, A. L.; Uversky, V. N. Conformational prerequisites for formation of amyloid fibrils from histones. J. Mol. Biol. 2004, 342, 1305-1324.
65. Luger, K.; Mader, A. W.; Richmond, R. K.; Sargent, D. F.; Richmond, T. J. Crystal structure of the nucleosome core particle at 2.8 A resolution. Nature 1997, 389, 251-260.
66. Arents, G.; Burlingame, R. W.; Wang, B. C.; Love, W. E.; Moudrianakis, E. N. The nucleosomal core histone octamer at 3.1 Å resolution: a tripartite protein assembly and a left-handed superhelix. Proc. Natl. Acad. Sci. U.S.A. 1991, 88, 10148-10152.
67. Hansen, J. C. Conformational dynamics of the chromatin fiber in solution: determinants, mechanisms, and functions. Annu. Rev. Biophys. Biomol. Struct. 2002, 31, 361-392.
68. Hansen, J. C.; Lu, X.; Ross, E. D.; Woody, R. W. Intrinsic protein disorder, amino acid composition, and histone terminal domains. J. Biol. Chem. 2006, 281, 1853-1856.
69. Walker, I. O. Differential dissociation of histone tails from core chromatin. Biochemistry 1984, 23, 5622-5628.
70. Mangenot, S.; Leforestier, A.; Vachette, P.; Durand, D.; Livolant, F. Salt-induced conformation and interaction changes of nucleosome core particles. Biophys. J. 2002, 82, 345-356.
71. Morgan, D. O. Principles of CDK regulation. Nature 1995, 374, 131-134.
72. Morgan, D. O. Cyclin-dependent kinases: engines, clocks, and microprocessors. Annu. Rev. Cell Dev. Biol. 1997, 13, 261-291.
73. Nigg, E. A. Mitotic kinases as regulators of cell division and its checkpoints. Nat. Rev. Mol. Cell Biol. 2001, 2, 21-32.
74. Pavletich, N. P. Mechanisms of cyclin-dependent kinase regulation: structures of Cdks, their cyclin activators, and Cip and INK4 inhibitors. J. Mol. Biol. 1999, 287, 821-828.
75. Kriwacki, R. W.; Hengst, L.; Tennant, L.; Reed, S. I.; Wright, P. E. Structural studies of p21Waf1/Cip1/Sdi1 in the free and Cdk2-bound state: conformational disorder mediates binding diversity. Proc. Natl. Acad. Sci. U.S.A. 1996, 93, 11504-11509.
76. Flaugh, S. L.; Lumb, K. J. Effects of macromolecular crowding on the intrinsically disordered proteins c-Fos and p27(Kip1). Biomacromolecules 2001, 2, 538-540.
77. Bienkiewicz, E. A.; Adkins, J. N.; Lumb, K. J. Functional consequences of preorganized helical structure in the intrinsically disordered cell-cycle inhibitor p27(Kip1). Biochemistry 2002, 41, 752-759.
78. Lacy, E. R.; Filippov, I.; Lewis, W. S.; Otieno, S.; Xiao, L.; Weiss, S.; Hengst, L.; Kriwacki, R. W. p27 binds cyclin-CDK complexes through a sequential mechanism involving binding-induced protein folding. Nat. Struct. Mol. Biol. 2004, 11, 358-364.
79. Adkins, J. N.; Lumb, K. J. Intrinsic structural disorder and sequence features of the cell cycle inhibitor p57Kip2. Proteins 2002, 46, 1-7.
80. Schmucker, D.; Clemens, J. C.; Shu, H.; Worby, C. A.; Xiao, J.; Muda, M.; Dixon, J. E.; Zipursky, S. L. Drosophila Dscam is an axon guidance receptor exhibiting extraordinary molecular diversity. Cell 2000, 101, 671-684.
81. Zhu, J.; Shendure, J.; Mitra, R. D.; Church, G. M. Single molecule profiling of alternative pre-mRNA splicing. Science 2003, 301, 836-838.
82. Tabuchi, K.; Sudhof, T. C. Structure and evolution of neurexin genes: insight into the mechanism of alternative splicing. Genomics 2002, 79, 849-859.
83. Jurica, M. S.; Moore, M. J. Pre-mRNA splicing: awash in a sea of proteins. Mol. Cell 2003, 12, 5-14.
84. Anderson, C. W.; Appella, E. Signaling to the p53 tumor suppressor through pathways activated by genotoxic and nongenotoxic stress. In Handbook of Cell Signaling; Bradshaw, R. A., Dennis, E. A., Eds.; Academic Press: New York, 2004; pp 237-247.
85. Hollstein, M.; Sidransky, D.; Vogelstein, B.; Harris, C. C. p53 mutations in human cancers. Science 1991, 253, 49-53.
86. Balint, E. E.; Vousden, K. H. Activation and activities of the p53 tumour suppressor protein. Br. J. Cancer 2001, 85, 1813-1823.
87. Zhao, R.; Gish, K.; Murphy, M.; Yin, Y.; Notterman, D.; Hoffman, W. H.; Tom, E.; Mack, D. H.; Levine, A. J. Analysis of p53-regulated gene expression patterns using oligonucleotide arrays. Genes Dev. 2000, 14, 981-993.
88. Bell, S.; Klein, C.; Muller, L.; Hansen, S.; Buchner, J. p53 contains large unstructured regions in its native state. J. Mol. Biol. 2002, 322, 917-927.
89. Lee, H.; Mok, K. H.; Muhandiram, R.; Park, K. H.; Suk, J. E.; Kim, D. H.; Chang, J.; Sung, Y. C.; Choi, K. Y.; Han, K. H. Local structural elements in the mostly unstructured transcriptional activation domain of human p53. J. Biol. Chem. 2000, 275, 29426-29432.
90. Dawson, R.; Muller, L.; Dehner, A.; Klein, C.; Kessler, H.; Buchner, J. The N-terminal domain of p53 is natively unfolded. J. Mol. Biol. 2003, 332, 1131-1141.
91. Kussie, P. H.; Gorina, S.; Marechal, V.; Elenbaas, B.; Moreau, J.; Levine, A. J.; Pavletich, N. P. Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain. Science 1996, 274, 948-953.
92. Rosal, R.; Pincus, M. R.; Brandt-Rauf, P. W.; Fine, R. L.; Michl, J.; Wang, H. NMR solution structure of a peptide from the mdm-2 binding domain of the p53 protein that is selectively cytotoxic to cancer cells. Biochemistry 2004, 43, 1854-1861.
93. Vargas, D. A.; Takahashi, S.; Ronai, Z. Mdm2: A regulator of cell growth and death. Adv. Cancer Res. 2003, 89, 1-34.
94. Ayed, A.; Mulder, F. A.; Yi, G. S.; Lu, Y.; Kay, L. E.; Arrowsmith, C. H. Latent and active p53 are identical in conformation. Nat. Struct. Biol. 2001, 8, 756-760.
95. Weinberg, R. L.; Freund, S. M.; Veprintsev, D. B.; Bycroft, M.; Fersht, A. R. Regulation of DNA binding of p53 by its C-terminal domain. J. Mol. Biol. 2004, 342, 801-811.
96. Cho, Y.; Gorina, S.; Jeffrey, P. D.; Pavletich, N. P. Crystal structure of a p53 tumor suppressor-DNA complex: understanding tumorigenic mutations. Science 1994, 265, 346-355.
97. Joerger, A. C.; Ang, H. C.; Veprintsev, D. B.; Blair, C. M.; Fersht, A. R. Structures of p53 cancer mutants and mechanism of rescue by second-site suppressor mutations. J. Biol. Chem. 2005, 280, 16030-16037.
98. Clore, G. M.; Ernst, J.; Clubb, R.; Omichinski, J. G.; Kennedy, W. M.; Sakaguchi, K.; Appella, E.; Gronenborn, A. M. Refined solution structure of the oligomerization domain of the tumour suppressor p53. Nat. Struct. Biol. 1995, 2 321-333.
99. Lee, W.; Harvey, T. S.; Yin, Y.; Yau, P.; Litchfield, D.; Arrowsmith, C. H. Solution structure of the tetrameric minimum transforming domain of p53. Nat. Struct. Biol. 1994, 1, 877-890.
100. Canadillas, J. M.; Tidow, H.; Freund, S. M.; Rutherford, T. J.; Ang, H. C.; Fersht, A. R. Solution structure of p53 core domain: structural basis for its instability. Proc. Natl. Acad. Sci. U.S.A. 2006, 103, 2109-2114.
101. Veprintsev, D. B.; Freund, S. M.; Andreeva, A.; Rutledge, S. E.; Tidow, H.; Canadillas, J. M.; Blair, C. M.; Fersht, A. R. Core domain interactions in full-length p53 in solution. Proc. Natl. Acad. Sci. U.S.A. 2006, 103, 2115-2119.
102. Hinds, M. G.; Day, C. L. Regulation of apoptosis: uncovering the binding determinants. Curr. Opin. Struct. Biol. 2005, 15, 690-699.
103. Puthalakath, H.; Strasser, A. Keeping killers on a tight leash: transcriptional and post-translational control of the pro-apoptotic activity of BH3-only proteins. Cell Death Differ. 2002, 9, 505-512.
104. Liu, X.; Dai, S.; Zhu, Y.; Marrack, P.; Kappler, J. W. The structure of a Bcl-xL/Bim fragment complex: implications for Bim function. Immunity 2003, 19, 341-352.
105. Sattler, M.; Liang, H.; Nettesheim, D.; Meadows, R. P.; Harlan, I. E.; Eberstadt, M.; Yoon, H. S.; Shuker, S. B.; Chang, B. S.; Minn, A. J.; Thompson, C. B.; Fesik, S. W. Structure of Bcl-xL-Bak peptide complex: recognition between regulators of apoptosis. Science 1997, 275, 983-986.
106. Petros, A. M.; Nettesheim, D. G.; Wang, Y.; Olejniczak, E. T.; Meadows, R. P.; Mack, J.; Swift, K.; Matayoshi, E. D.; Zhang, H.; Thompson, C. B.; Fesik, S. W. Rationale for Bcl-xL/Bad peptide complex formation from structure, mutagenesis, and biophysical studies. Protein Sci. 2000, 9, 2528-2534.
107. Yan, N.; Gu, L.; Kokel, D.; Chai, J.; Li, W.; Han, A.; Chen, L.; Xue, D.; Shi, Y. Structural, biochemical, and functional analyses of CED-9 recognition by the proapoptotic proteins EGL-1 and CED-4. Mol. Cell 2004, 15, 999-1006.
108. Fan, J.; Zhang, Q.; Tochio, H.; Li, M.; Zhang, M. Structural basis of diverse sequence-dependent target recognition by the 8 kDa dynein light chain. J. Mol. Biol. 2001, 306, 97-108.
109. Hinds, M. G.; Smits, C.; Fredericks-Short, R.; Risk, J. M.; Bailey, M.; Huang, D. C.; Day, C. L. Bim, Bad and Bmf: intrinsically unstructured BH3-only proteins that undergo a localized conformational change upon binding to prosurvival Bcl-2 targets. Cell Death Differ. 2006, 14, 128-136.
110. Oldfield, C. I.; Cheng, Y.; Cortese, M. S.; Romero, P.; Uversky, V. N.; Dunker, A. K. Coupled folding and binding with α-helix-forming molecular recognition elements. Biochemistry 2005, 44, 12454-12470.
111. Huang, D. T.; Walden, H.; Duda, D.; Schulman, B. A. Ubiquitin-like protein activation. Oncogene 2004, 23, 1958-1971.
112. Hay, R. T. Role of ubiquitin-like proteins in transcriptional regulation. Ernst Schering Res. Found. Workshop 2006, 173-192.
113. Catic, A.; Collins, C.; Church, G. M.; Ploegh, H. L. Preferred in vivo ubiquitination sites. Bioinformatics 2004, 20, 3302-3307.
114. Macauley, M. S.; Errington, W. J.; Scharpf, M.; Mackereth, C. D.; Blaszczak, A. G.; Graves, B. J.; McIntosh, L. P. Beads-on-a-string, characterization of ETS-1 sumoylated within its flexible N-terminal sequence. J. Biol. Chem. 2006, 281, 4164-4172.
115. Logan, C. Y.; Nusse, R. The Wnt signaling pathway in development and disease. Annu. Rev. Cell Dev. Biol. 2004, 20, 781-810.
116. Kelleher, F. C.; Fennelly, D.; Rafferty, M. Common critical pathways in embryogenesis and cancer. Acta Oncol. 2006, 45, 375-388.
117. Clevers, H. Wnt/beta-catenin signaling in development and disease. Cell 2006, 127, 469-480.
118. Prud'homme, B.; Lartillot, N.; Balavoine, G.; Adoutte, A.; Vervoort, M. Phylogenetic analysis of the Wnt gene family. Insights from lophotrochozoan members. Curr. Biol. 2002, 12, 1395.
119. Kusserow, A.; Pang, K.; Sturm, C.; Hrouda, M.; Lentfer, J.; Schmidt, H. A.; Technau, U.; von Haeseler, A.; Hobmayer, B.; Martindale, M. Q.; Holstein, T. W. Unexpected complexity of the Wnt gene family in a sea anemone. Nature 2005, 433, 156-160.
120. Gordon, M. D.; Nusse, R. Wnt signaling: multiple pathways, multiple receptors, and multiple transcription factors. J. Biol. Chem. 2006, 281, 22429-22433.
121. Moon, R. T.; Bowerman, B.; Boutros, M.; Perrimon, N. The promise and perils of Wnt signaling through beta-catenin. Science 2002, 296, 1644-1646.
122. Kohn, A. D.; Moon, R. T. Wnt and calcium signaling: beta-catenin- independent pathways. Cell Calcium 2005, 38, 439-446.
123. Katoh, M.; Kirikoshi, H.; Saitoh, T.; Sagara, N.; Koike, J. Alternative splicing of the WNT-2B/WNT-13 gene. Biochem. Biophys. Res. Commun. 2000, 275, 209-216.
124. Pospisil, H.; Herrmann, A.; Butherus, K.; Pirson, S.; Reich, J. G.; Kemmner, W. Verification of predicted alternatively spliced Wnt genes reveals two new splice variants (CTNNB1 and LRP5) and altered Axin-1 expression during tumour progression. BMC Genomics 2006, 7, 148.
125. Struewing, I. T.; Toborek, A.; Mao, C. D. Mitochondrial and nuclear forms of Wnt13 are generated via alternative promoters, alternative RNA splicing, and alternative translation start sites. J. Biol. Chem. 2006, 281, 7282-7293.
126. Ding, Y.; Dale, T. Wnt signal transduction: kinase cogs in a nano-machine? Trends Biochem. Sci. 2002, 27, 327-329.
127. Dajani, R.; Fraser, E.; Roe, S. M.; Young, N.; Good, V.; Dale, T. C.; Pearl, L. H. Crystal structure of glycogen synthase kinase 3 beta: structural basis for phosphate-primed substrate specificity and autoinhibition. Cell 2001, 105, 721-732.
128. Apuzzo, S.; Gros, P. The paired domain of pax3 contains a putative homeodomain interaction pocket defined by cysteine scanning mutagenesis. Biochemistry 2006, 45, 7154-7161.
129. Haubst, N.; Berger, J.; Radjendirane, V.; Graw, J.; Favor, J.; Saunders, G. F.; Stoykova, A.; Gotz, M. Molecular dissection of Pax6 function: the specific roles of the paired domain and homeodomain in brain development. Development 2004, 131, 6131-6140.
130. Zhang, F.; Nakanishi, G.; Kurebayashi, S.; Yoshino, K.; Perantoni, A.; Kim, Y. S.; Jetten, A. M. Characterization of Glis2, a novel gene encoding a Gli-related, Kruppel-like transcription factor with transactivation and repressor functions. Roles in kidney development and neurogenesis. J. Biol. Chem. 2002, 277, 10139-10149.
131. Paratore, C.; Brugnoli, G.; Lee, H. Y.; Suter, U.; Sommer, L. The role of the Ets domain transcription factor Erm in modulating differentiation of neural crest stem cells. Dev. Biol. 2002, 250, 168-180.
132. Chalepakis, G.; Wijnholds, J.; Gruss, P. Pax-3-DNA interaction: flexibility in the DNA binding and induction of DNA conformational changes by paired domains. Nucleic Acids Res. 1994, 22, 3131-3137.
133. Mishra, R.; Gorlov, I. P.; Chao, L. Y.; Singh, S.; Saunders, G. F. PAX6, paired domain influences sequence recognition by the homeodomain. J. Biol. Chem. 2002, 277, 49488-49494.
134. Mauen, S.; Huvent, I.; Raussens, V.; Demonte, D.; Baert, J. L.; Tricot, C.; Ruysschaert, J. M.; Van Lint, C.; Moguilevsky, N.; de Launoit, Y. Expression, purification, and structural prediction of the Ets transcription factor ERM. Biochim. Biophys. Acta 2006, 1760, 1192-1201.
135. Hiraga, S. Chromosome partition in Escherichia coli. Curr. Opin. Genet. Dev. 1993, 3, 789-801.
136. Melby, T. E.; Ciampaglio, C. N.; Briscoe, G.; Erickson, H. P. The symmetrical structure of structural maintenance of chromosomes (SMC) and MukB proteins: long, antiparallel coiled coils, folded at a flexible hinge. J. Cell Biol. 1998, 142, 1595-1604.
137. James, L. C.; Tawfik, D. S. Conformational diversity and protein evolution - a 60-year-old hypothesis revisited. Trends Biochem. Sci. 2003, 28, 361-368.
138. Pauling, L. A theory of the structure and process of formation of antibodies. J. Am. Chem. Soc. 1940, 62, 2643-2657.
139. Carl, P. L.; Temple, B. R.; Cohen, P. L. Most nuclear systemic autoantigens are extremely disordered proteins: implications for the etiology of systemic autoimmunity. Arthritis Res. Ther. 2005, 7, R1360-1374.
140. Slutzki, M.; Jaitin, D. A.; Yehezkel, T. B.; Schreiber, G. Variations in the unstructured c-terminal tail of interferons contribute to differential receptor binding and biological activity. J. Mol. Biol. 2006, 360, 1019-1030.
141. Sigalov, A. B. Multichain immune recognition receptor signaling: different players, same game? Trends Immunol. 2004, 25, 583-589.
142. Sigalov, A. B. Immune cell signaling: a novel mechanistic model reveals new therapeutic targets. Trends Pharmacol. Sci. 2006, 27, 518-524.
143. Sigalov, A. Multi-chain immune recognition receptors: spatial organization and signal transduction. Semin. Immunol. 2005, 17, 51-64.
144. Sigalov, A. B.; Aivazian, D. A.; Uversky, V. N.; Stern, L. J. Lipid-binding activity of intrinsically unstructured cytoplasmic domains of multichain immune recognition receptor signaling subunits. Biochemistry 2006, 45, 15731-15739.
145. Sigalov, A.; Aivazian, D.; Stern, L. Homooligomerization of the cytoplasmic domain of the T cell receptor zeta chain and of other proteins containing the immunoreceptor tyrosine-based activation motif. Biochemistry 2004, 43, 2049-2061.
146. Sigalov, A. B.; Zhuravleva, A. V.; Orekhov, V. Y. Binding of intrinsically disordered proteins is not necessarily accompanied by a structural transition to a folded form. Biochimie 2006, in press.
147. Wehner, K. A.; Baserga, S. J. The sigma(70)-like motif: a eukaryotic RNA binding domain unique to a superfamily of proteins required for ribosome biogenesis. Mol. Cell 2002, 9, 329-339.
148. Dragon, F.; Gallagher, J. E.; Compagnone-Post, P. A.; Mitchell, B. M.; Porwancher, K. A.; Wehner, K. A.; Wormsley, S.; Settlage, R. E.; Shabanowitz, J.; Osheim, Y.; Beyer, A. L.; Hunt, D. F.; Baserga, S. J. A large nucleolar U3 ribonucleoprotein required for 18S ribosomal RNA biogenesis. Nature 2002, 417, 967-970.
149. Hernandez, V. P.; Higgins, L.; Schwientek, M. S.; Fallon, A. M. The histone-like C-terminal extension in ribosomal protein S6 in Aedes and Anopheles mosquitoes is encoded within the distal portion of exon 3. Insect Biochem. Mol. Biol. 2003, 33, 901-910.
150. Chung, S.; McLean, M. R.; Rymond, B. C. Yeast ortholog of the Drosophila crooked neck protein promotes spliceosome assembly through stable U4/U6.U5 snRNP addition. RNA 1999, 5, 1042-1054.
151. Abe, Y.; Shodai, T.; Muto, T.; Mihara, K.; Torii, H.; Nishikawa, S.; Endo, T.; Kohda, D. Structural basis of presequence recognition by the mitochondrial protein import receptor Tom20. Cell 2000, 100, 551-560.
152. Olsen, B. R.; Reginato, A. M.; Wang, W. Bone development. Annu. Rev. Cell Dev. Biol. 2000, 16, 191-220.
153. Goldring, M. B.; Tsuchimochi, K.; Ijiri, K. The control of chondrogenesis. J. Cell. Biochem. 2006, 97, 33-44.
154. Tickle, C. Molecular basis of vertebrate limb patterning. Am. J. Med. Genet. 2002, 112, 250-255.
155. Yoshida, C. A.; Komori, T. Role of Runx proteins in chondrogenesis. Crit. Rev. Eukaryotic Gene Expression 2005, 15, 243-254.
156. Morita, N.; Kiryu, S.; Kiyama, H. p53-independent cyclin G expression in a group of mature neurons and its enhanced expression during nerve regeneration. J. Neurosci. 1996, 16, 5961-5966.
157. Skotzko, M.; Wu, L.; Anderson, W. F.; Gordon, E. M.; Hall, F. L. Retroviral vector-mediated gene transfer of antisense cyclin G1 (CYCG1) inhibits proliferation of human osteogenic sarcoma cells. Cancer Res. 1995, 55, 5493-5498.
158. Kanaoka, Y.; Kimura, S. H.; Okazaki, I.; Ikeda, M.; Nojima, H. GAK: a cyclin G associated kinase contains a tensin/auxilin-like domain. FEBS Lett. 1997, 402, 73-80.
159. Okamoto, K.; Kamibayashi, C; Serrano, M.; Prives, C; Mumby, M. C; Beach, D. p53-dependent association between cyclin G and the B′ subunit of protein phosphatase 2A. Mol. Cell. Biol. 1996, 16, 6593-6602.
160. Okamoto, K.; Beach, D. Cyclin G is a transcriptional target of the p53 tumor suppressor protein. EMBO J. 1994, 13, 4816-4822.
161. Williamson, J. R. Induced fit in RNA-protein recognition. Nat. Struct. Biol. 2000, 7, 834-837.
162. Leulliot, N.; Varani, G. Current topics in RNA-protein recognition: control of specificity and biological function through induced fit and conformational capture. Biochemistry 2001, 40, 7947-7956.
163. Chen, Y; Varani, G. Protein families and RNA recognition. Febs J. 2005, 272, 2088-2097.
164. Crowder, S. M.; Kanaar, R.; Rio, D. C; Alber, T. Absence of interdomain contacts in the crystal structure of the RNA recognition motifs of Sex-lethal. Proc. Natl. Acad. Sci. USA. 1999, 96, 4892-4897.
165. Torres-Larios, A.; Swinger, K. K.; Pan, T.; Mondragon, A. Structure of ribonuclease P - a universal ribozyme. Curr. Opin. Struct. Biol. 2006, 16, 327-335.
166. Harris, M. E.; Christian, E. L. Recent insights into the structure and function of the ribonucleoprotein enzyme ribonuclease P. Curr. Opin. Struct. Biol. 2003, 13, 325-333.
167. Guo, X.; Campbell, F. E.; Sun, L.; Christian, E. L.; Anderson, V. E.; Harris, M. E. RNA-dependent folding and stabilization of C5 protein during assembly of the E. coli RNase P holoenzyme. J. Mol Biol. 2006, 360, 190-203.
168. Henkels, C. H.; Kurz, J. C; Fierke, C. A.; Oas, T. G. Linked folding and anion binding of the Bacillus subtilis ribonuclease P protein. Biochemistry 2001, 40, 2777-2789.
169. Nissen, P.; Hansen, J.; Ban, N.; Moore, P. B.; Steitz, T. A. The structural basis of ribosome activity in peptide bond synthesis. Science 2000, 289, 920-930.
170. Recht, M. I.; Williamson, J. R. RNA tertiary structure and cooperative assembly of a large ribonucleoprotein complex. J. Mol. Biol. 2004, 344, 395-407.
171. Schroeder, R.; Barta, A.; Semrad, K. Strategies for RNA folding and assembly. Nat. Rev. Mol. Cell Biol. 2004, 5, 908-919.
172. Klein, D. J.; Moore, P. B.; Steitz, T. A. The roles of ribosomal proteins in the structure assembly, and evolution of the large ribosomal subunit. J. Mol. Biol. 2004, 340, 141-177.
173. Deutsch, H. F. Chemistry and biology of alpha-fetoprotein. Adv. Cancer Res. 1991, 56, 253-312.
174. Gillespie, J. R.; Uversky, V. N. Structure and function of alpha-fetoprotein: a biophysical overview. Biochim. Biophys. Acta 2000, 1480, 41-56.
175. Kossiakoff, A. A. The structural basis for biological signaling, regulation, and specificity in the growth hormone-prolactin system of hormones and receptors. Adv. Protein Chem. 2004, 68, 147-169.
176. Gronwald, W.; Schomburg, D.; Tegge, W.; Wray, V. Assessment by 1H NMR spectroscopy of the structural behaviour of human parathyroid-hormone-related protein(1-34) and its close relationship with the N-terminal fragments of human parathyroid hormone in solution. Biol. Chem. 1997, 378, 1501-1508.
177. Gronenborn, A. M.; Bovermann, G.; Clore, G. M. A 1H-NMR study of the solution conformation of secretin. Resonance assignment and secondary structure. FEBS Lett. 1987, 215, 88-94.
178. De, Silva, R. S.; Kovacikova, G.; Lin, W.; Taylor, R. K.; Skorupski, K.; Kull, F. J. Crystal structure of the virulence gene activator AphA from Vibrio cholerae reveals it is a novel member of the winged helix transcription factor superfamily. J. Biol. Chem. 2005, 280, 13779-13783.
179. Lewis, M.; Chang, G.; Horton, N. C; Kercher, M. A.; Pace, H. C; Schumacher, M. A.; Brennan, R. G.; Lu, P. Crystal structure of the lactose operon repressor and its complexes with DNA and inducer. Science 1996, 271, 1247-1254.
180. Hedrick, J. A.; Zlotnik, A. Lymphotactin: a new class of chemokine. Methods Enzymol 1997, 287, 206-215.
181. Marcaurelle, L. A.; Mizoue, L. S.; Wilken, J.; Oldham, L.; Kent, S. B.;
182. Kuloglu, E. S.; McCaslin, D. R.; Markley, J. L.; Volkman, B. F. Structural rearrangement of human lymphotactin, a C chemokine, under physiological solution conditions. J. Biol. Chem. 2002, 277, 17863-17870.
183. Smyth, E.; Syme, C. D.; Blanch, E. W.; Hecht, L.; Vasak, M.; Barron, L. D. Solution structure of native proteins with irregular folds from Raman optical activity. Biopolymers 2001, 58, 138-151.
184. Ennahar, S.; Sashihara, T.; Sonomoto, K.; Ishizaki, A. Class Ha bacteriocins: biosynthesis, structure and activity. FEMS Microbiol. Rev. 2000, 24, 85-106.
185. Eijsink, V. G.; Axelsson, L.; Diep, D. B.; Havarstein, L. S.; Holo, H.; Nes, I. F. Production of class II bacteriocins by lactic acid bacteria; an example of biological warfare and communication. Antonie Van Leeuwenhoek 2002, 81, 639-654.
186. Kaur, K.; Andrew, L. C; Wishart, D. S.; Vederas, J. C. Dynamic relationships among type Ha bacteriocins: temperature effects on antimicrobial activity and on structure of the C-terminal amphipathic α helix as a receptor-binding region. Biochemistry 2004, 43, 9009-9020.
187. Prates, M. V.; Sforca, M. L.; Regis, W. C; Leite, J. R.; Silva, L. P.; Pertinhez, T. A.; Araujo, A. L.; Azevedo, R. B.; Spisni, A.; Bloch, C, Jr. The NMR-derived solution structure of a new cationic antimicrobial peptide from the skin secretion of the anuran Hyla punctata. J. Biol Chem. 2004, 279, 13018-13026.
188. Miyata, A.; Arimura, A.; Dahl, R. R.; Minamino, N.; Uehara, A.; liang, L.; Culler, M. D.; Coy, D. H. Isolation of a novel 38 residue-hypothalamic polypeptide which stimulates adenylate cyclase in pituitary cells. Biochem. Biophys. Res. Commun. 1989,164, 567-574.
189. Arimura, A. Pituitary adenylate cyclase activating polypeptide (PACAP): discovery and current status of research. Regul Pept. 1992, 37, 287-303.
190. Wray, V.; Kakoschke, C; Nokihara, K.; Naruse, S. Solution structure of pituitary adenylate cyclase activating polypeptide by nuclear magnetic resonance spectroscopy. Biochemistry 1993, 32, 5832-5841.
191. Cai, X.; Dass, C. Structural characterization of methionine and leucine enkephalins by hydrogen/deuterium exchange and electrospray ionization tandem mass spectrometry. Rapid Commun. Mass Spectrom. 2005, 19, 1-8.
192. Takai, Y.; Sasaki, T.; Matozaki, T. Small GTP-binding proteins. Physiol. Rev. 2001, 81 153-208.
193. Symons, M.; Settleman, J. Rho family GTPases: more than simple switches. Trends Cell Biol. 2000, 10, 415-419.
194. Scheffzek, K.; Ahmadian, M. R. GTPase activating proteins: structural and functional insights 18 years after discovery. Cell Mol. Life Sci. 2005, 62, 3014-3038.
195. Bernards, A. GAPs galore! A survey of putative Ras superfamily GTPase activating proteins in man and Drosophila. Biochim. Biophys. Acta 2003, 1603, 47-82.
196. Bernards, A.; Settleman, J. GAP control: regulating the regulators of small GTPases. Trends Cell Biol. 2004, 14, 377-385.
197. Grosschedl, R.; Giese, K.; Pagel, J. HMG domain proteins: architectural elements in the assembly of nucleoprotein structures. Trends Genet. 1994, 10, 94-100.
198. Reeves, R.; Beckerbauer, L. HMGI/Y proteins: flexible regulators of transcription and chromatin structure. Biochim. Biophys. Acta 2001, 1519, 13-29.
199. Lehn, D. A.; Elton, T. S.; Johnson, K. R.; Reeves, R. A conformational study of the sequence specific binding of HMG-I (Y) with the bovine interleukin-2 cDNA. Biochem. Int. 1988,16, 963-971.
200. Evans, J. N.; Nissen, M. S.; R. R. Assignment of the 1H NMR spectrum of a consensus DNA-binding peptide from the HMG-I protein. Bull. Magn. Reson. 1992, 14, 171-174.
201. Evans, J. N.; Zajicek, J.; Nissen, M. S.; Munske, G.; Smith, V.; Reeves, R. 1H and 13C NMR assignments and molecular modelling of a minor groove DNA-binding peptide from the HMG-I protein. Int. J. Pept. Protein Res. 1995, 45, 554-560.
202. Conti, B.; Tabarean, I.; Andrei, C; Bartfai, T. Cytokines and fever. Front. Biosci. 2004, 9, 1433-1449.
203. Janecka, A.; Kruszynski, R. Conformationally restricted peptides as tools in opioid receptor studies. Curr. Med. Chem. 2005, 12, 471-481.
204. Chaturvedi, K.; Christoffers, K. H.; Singh, K.; Howells, R. D. Structure and regulation of opioid receptors. Biopolymers 2000, 55, 334-346.
205. 1H NMR spectroscopy. Biochemistry 1987, 26, 5916-5925.
206. Tsunemi, M.; Kato, H.; Nishiuchi, Y.; Kumagaye, S.; Sakakibara, S. Synthesis and structure-activity relationships of elafin, an elastase-specific inhibitor. Biochem. Biophys. Res. Commun. 1992, 185, 967-973.
207. Francart, G.; Dauchez, M.; Alix, A. J.; Lippens, G. Solution structure of R-elafin, a specific inhibitor of elastase. J. Mol. Biol. 1997, 268, 666-677.
208. Rusnak, F.; Mertz, P. Calcineurin: form and function. Physiol Rev. 2000, 80, 1483-1521.
209. Kissinger, C. R.; Parge, H. E.; Knighton, D. R.; Lewis, C. T.; Pelletier, L. A.; Tempczyk, A.; Kalish, V. J.; Tucker, K. D.; Showalter, R. E.; Moomaw, E. W.; et al. Crystal structures of human calcineurin and the human FKBP12-FK506-calcineurin complex. Nature 1995, 378, 641-644.
210. Delcour, A. H. Structure and function of pore-forming beta-barrels from bacteria. J. Mol. Microbiol. Biotechnol. 2002, 4, 1-10.
211. Sukumaran, S.; Hauser, K.; Maier, E.; Benz, R.; Mantele, W. Structure-function correlation of outer membrane protein porin from Paracoccus denitrificans. Biopolymers 2006, 82, 344-348.
212. Sukumaran, S.; Hauser, K.; Maier, E.; Benz, R.; Mantele, W. Tracking the unfolding and refolding pathways of outer membrane protein porin from Paracoccus denitrificans. Biochemistry 2006, 45, 3972-3980.
213. Violot, S.; Aghajari, N.; Czjzek, M.; Feller, G.; Sonan, G. K.; Gouet, P.; Gerday, C; Haser, R.; Receveur-Brechot, V. Structure of a full length psychrophilic cellulase from Pseudoalteromonas haloplanktis revealed by X-ray diffraction and small angle X-ray scattering. J. Mol. Biol 2005, 348, 1211-1224.
214. von Ossowski, I.; Eaton, J. T.; Czjzek, M.; Perkins, S. J.; Frandsen, T. P.; Schulein, M.; Panine, P.; Henrissat, B.; Receveur-Brechot, V. Protein disorder: conformational distribution of the flexible linker in a chimeric double cellulase. Biophys. J. 2005, 88, 2823-2832.
215. Bordelon, T.; Montegudo, S. K.; Pakhomova, S.; Oldham, M. L.; Newcomer, M. E. A disorder to order transition accompanies catalysis in retinaldehyde dehydrogenase type II. J. Biol. Chem. 2004, 279, 43085-43091.
216. Iakoucheva, L. M.; Radivojac, P.; Brown, C. J.; O'Connor, T. R.; Sikes, J. G.; Obradovic, Z.; Dunker, A. K. The importance of intrinsic disorder for protein phosphorylation. Nucleic Acids Res. 2004, 32, 1037-1049.