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Volumn 27, Issue 10, 2002, Pages 521-526

Intramolecular interactions at protein surfaces and their impact on protein function

Author keywords

[No Author keywords available]

Indexed keywords

BARNASE; COLD SHOCK PROTEIN; FIBRONECTIN; PROTEIN; PROTEIN U1A; RIBONUCLEASE A; RNA; SINGLE STRANDED DNA; TRANSCRIPTION FACTOR GCN4; UNCLASSIFIED DRUG; XYLAN ENDO 1,3 BETA XYLOSIDASE;

EID: 0036805481     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0968-0004(02)02184-9     Document Type: Review
Times cited : (20)

References (54)
  • 1
    • 0032548904 scopus 로고    scopus 로고
    • Adaptation of protein surfaces to subcellular location
    • Andrade M.A., et al. Adaptation of protein surfaces to subcellular location. J. Mol. Biol. 276:1998;517-525.
    • (1998) J. Mol. Biol. , vol.276 , pp. 517-525
    • Andrade, M.A.1
  • 2
    • 0034177264 scopus 로고    scopus 로고
    • Antagonists of protein-protein interactions
    • Cochran A.G. Antagonists of protein-protein interactions. Chem. Biol. 7:2000;R85-R94.
    • (2000) Chem. Biol. , vol.7
    • Cochran, A.G.1
  • 3
    • 0037061646 scopus 로고    scopus 로고
    • Inhibition of protein-protein association by small molecules: Approaches and progress
    • Toogood P.L. Inhibition of protein-protein association by small molecules: approaches and progress. J. Med. Chem. 45:2002;1543-1558.
    • (2002) J. Med. Chem. , vol.45 , pp. 1543-1558
    • Toogood, P.L.1
  • 5
    • 12944281813 scopus 로고    scopus 로고
    • Structure-based design of an osteoclast-selective nonpeptide Src homology 2 inhibitor with in vivo antiresorptive activity
    • Shakespeare W., et al. Structure-based design of an osteoclast-selective nonpeptide Src homology 2 inhibitor with in vivo antiresorptive activity. Proc. Natl. Acad. Sci. U. S. A. 97:2000;9373-9378.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 9373-9378
    • Shakespeare, W.1
  • 6
    • 0033757840 scopus 로고    scopus 로고
    • From structure to function: Approaches and limitations
    • Thornton J.M., et al. From structure to function: approaches and limitations. Nat. Struct. Biol. 7:2000;991-994.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 991-994
    • Thornton, J.M.1
  • 7
    • 0035141353 scopus 로고    scopus 로고
    • Dynamical view of the positions of key side chains in protein-protein recognition
    • Kimura S.R., et al. Dynamical view of the positions of key side chains in protein-protein recognition. Biophys. J. 80:2001;635-642.
    • (2001) Biophys. J. , vol.80 , pp. 635-642
    • Kimura, S.R.1
  • 8
    • 0036606483 scopus 로고    scopus 로고
    • Principles of docking: An overview of search algorithms and a guide to scoring functions
    • Halperin I., et al. Principles of docking: An overview of search algorithms and a guide to scoring functions. Proteins. 47:2002;409-443.
    • (2002) Proteins , vol.47 , pp. 409-443
    • Halperin, I.1
  • 9
    • 0032897494 scopus 로고    scopus 로고
    • An analysis of conformational changes on protein-protein associations: Implications for predictive docking
    • Betts M.J., Sternberg M.J.E. An analysis of conformational changes on protein-protein associations: Implications for predictive docking. Protein Eng. 12:1999;271-283.
    • (1999) Protein Eng. , vol.12 , pp. 271-283
    • Betts, M.J.1    Sternberg, M.J.E.2
  • 10
    • 0031746754 scopus 로고    scopus 로고
    • Statistical thermodynamic linkage between conformational and binding equilibria
    • Freire E. Statistical thermodynamic linkage between conformational and binding equilibria. Adv. Protein Chem. 51:1998;255-279.
    • (1998) Adv. Protein Chem. , vol.51 , pp. 255-279
    • Freire, E.1
  • 11
    • 0033784534 scopus 로고    scopus 로고
    • Induced fit in RNA-protein recognition
    • Williamson J.R. Induced fit in RNA-protein recognition. Nat. Struct. Biol. 7:2000;834-837.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 834-837
    • Williamson, J.R.1
  • 12
    • 0015222647 scopus 로고
    • The interpretation of protein structures: Estimation of static accessibility
    • Lee B., 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
  • 13
    • 0015866154 scopus 로고
    • Environment and exposure to solvent of protein atoms. Lysozyme and insulin
    • Shrake A., Rupley J.A. Environment and exposure to solvent of protein atoms. Lysozyme and insulin. J. Mol. Biol. 79:1973;351-371.
    • (1973) J. Mol. Biol. , vol.79 , pp. 351-371
    • Shrake, A.1    Rupley, J.A.2
  • 14
    • 0023645203 scopus 로고
    • Interior and surface of monomeric proteins
    • Miller S., et al. Interior and surface of monomeric proteins. J. Mol. Biol. 196:1987;641-656.
    • (1987) J. Mol. Biol. , vol.196 , pp. 641-656
    • Miller, S.1
  • 15
    • 0000372879 scopus 로고    scopus 로고
    • Protein-protein interactions: Interface structure, binding thermodynamics, and mutational analysis
    • Stites W.E. Protein-protein interactions: interface structure, binding thermodynamics, and mutational analysis. Chem. Rev. 97:1997;1233-1250.
    • (1997) Chem. Rev. , vol.97 , pp. 1233-1250
    • Stites, W.E.1
  • 16
    • 0032479179 scopus 로고    scopus 로고
    • Anatomy of hot spots in protein interfaces
    • Bogan A.A., Thorn K.S. Anatomy of hot spots in protein interfaces. J. Mol. Biol. 280:1998;1-9.
    • (1998) J. Mol. Biol. , vol.280 , pp. 1-9
    • Bogan, A.A.1    Thorn, K.S.2
  • 17
    • 0003187567 scopus 로고    scopus 로고
    • The atomic structure of protein-protein recognition sites
    • LoConte L., et al. The atomic structure of protein-protein recognition sites. J. Mol. Biol. 285:1999;2177-2198.
    • (1999) J. Mol. Biol. , vol.285 , pp. 2177-2198
    • LoConte, L.1
  • 18
    • 0019837215 scopus 로고
    • Nature of the charge distribution in proteins
    • Wada A., Nakamura H. Nature of the charge distribution in proteins. Nature. 293:1981;757-758.
    • (1981) Nature , vol.293 , pp. 757-758
    • Wada, A.1    Nakamura, H.2
  • 20
    • 0025789054 scopus 로고
    • Side-chain clusters in protein structures and their role in protein folding
    • Heringa J., Argos P. Side-chain clusters in protein structures and their role in protein folding. J. Mol. Biol. 220:1991;151-171.
    • (1991) J. Mol. Biol. , vol.220 , pp. 151-171
    • Heringa, J.1    Argos, P.2
  • 21
    • 0344457301 scopus 로고    scopus 로고
    • Spatial sign-alternating charge clusters in globular proteins
    • Chirgadze Y.N., Larionova E.A. Spatial sign-alternating charge clusters in globular proteins. Protein Eng. 12:1999;101-105.
    • (1999) Protein Eng. , vol.12 , pp. 101-105
    • Chirgadze, Y.N.1    Larionova, E.A.2
  • 22
    • 0035448574 scopus 로고    scopus 로고
    • Ion pairs and thermotolerance of proteins from hyperthermophiles: A'traffic' rule for hot roads
    • Karshikoff A., Ladenstein R. Ion pairs and thermotolerance of proteins from hyperthermophiles: a'traffic' rule for hot roads. Trends Biochem. Sci. 26:2001;550-556.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 550-556
    • Karshikoff, A.1    Ladenstein, R.2
  • 23
    • 0029070109 scopus 로고
    • Conserved structural features at protein surfaces: Small exterior hydrophobic clusters
    • Tisi L.C., Evans P.A. Conserved structural features at protein surfaces: small exterior hydrophobic clusters. J. Mol. Biol. 249:1995;251-258.
    • (1995) J. Mol. Biol. , vol.249 , pp. 251-258
    • Tisi, L.C.1    Evans, P.A.2
  • 24
    • 0034495733 scopus 로고    scopus 로고
    • Aromatic clusters: A determinant of thermal stability of thermophilic proteins
    • Kannan N., Vishveshwara S. Aromatic clusters: a determinant of thermal stability of thermophilic proteins. Protein Eng. 13:2000;753-761.
    • (2000) Protein Eng. , vol.13 , pp. 753-761
    • Kannan, N.1    Vishveshwara, S.2
  • 25
    • 0025663105 scopus 로고
    • Strength and cooperativity of contributions of surface salt bridges to protein stability
    • Horovitz A., et al. Strength and cooperativity of contributions of surface salt bridges to protein stability. J. Mol. Biol. 216:1990;1031-1044.
    • (1990) J. Mol. Biol. , vol.216 , pp. 1031-1044
    • Horovitz, A.1
  • 26
    • 0033554840 scopus 로고    scopus 로고
    • Engineering a thermostable protein via optimization of charge-charge interactions on the protein surface
    • Loladze V.V., et al. Engineering a thermostable protein via optimization of charge-charge interactions on the protein surface. Biochemistry. 38:1999;16419-16423.
    • (1999) Biochemistry , vol.38 , pp. 16419-16423
    • Loladze, V.V.1
  • 27
    • 0032872888 scopus 로고    scopus 로고
    • Increasing protein stability by altering long-range coulombic interactions
    • Grimsley G.R., et al. Increasing protein stability by altering long-range coulombic interactions. Protein Sci. 8:1999;1843-1849.
    • (1999) Protein Sci. , vol.8 , pp. 1843-1849
    • Grimsley, G.R.1
  • 28
    • 0034673153 scopus 로고    scopus 로고
    • Contribution of surface salt bridges to protein stability
    • Strop P., Mayo S.L. Contribution of surface salt bridges to protein stability. Biochemistry. 39:2000;1251-1255.
    • (2000) Biochemistry , vol.39 , pp. 1251-1255
    • Strop, P.1    Mayo, S.L.2
  • 29
    • 0034620528 scopus 로고    scopus 로고
    • Rational modification of protein stability by the mutation of charged surface residues
    • Spector S., et al. Rational modification of protein stability by the mutation of charged surface residues. Biochemistry. 39:2000;872-879.
    • (2000) Biochemistry , vol.39 , pp. 872-879
    • Spector, S.1
  • 30
    • 0035964254 scopus 로고    scopus 로고
    • Stabilization of fibronectin type III domain by the removal of unfavorable electrostatic interactions on the protein surface
    • Koide A., et al. Stabilization of fibronectin type III domain by the removal of unfavorable electrostatic interactions on the protein surface. Biochemistry. 40:2001;10326-10333.
    • (2001) Biochemistry , vol.40 , pp. 10326-10333
    • Koide, A.1
  • 31
    • 0036228118 scopus 로고    scopus 로고
    • Distance dependence and salt sensitivity of pairwise coulombic interactions in a protein
    • Lee K.K., et al. Distance dependence and salt sensitivity of pairwise coulombic interactions in a protein. Protein Sci. 11:2002;1004-1016.
    • (2002) Protein Sci. , vol.11 , pp. 1004-1016
    • Lee, K.K.1
  • 32
    • 0037129945 scopus 로고    scopus 로고
    • Electrostatic interactions in ubiquitin: Stabilization of carboxylates by lysine amino groups
    • Sundd M., et al. Electrostatic interactions in ubiquitin: stabilization of carboxylates by lysine amino groups. Biochemistry. 41:2002;7586-7596.
    • (2002) Biochemistry , vol.41 , pp. 7586-7596
    • Sundd, M.1
  • 33
    • 0033852796 scopus 로고    scopus 로고
    • Charge-charge interactions influence the denatured state ensemble and contribute to protein stability
    • Pace C.N., et al. Charge-charge interactions influence the denatured state ensemble and contribute to protein stability. Protein Sci. 9:2000;1395-1398.
    • (2000) Protein Sci. , vol.9 , pp. 1395-1398
    • Pace, C.N.1
  • 34
    • 0034100848 scopus 로고    scopus 로고
    • Two exposed amino acid residues confer thermostability on a cold shock protein
    • Perl D., et al. Two exposed amino acid residues confer thermostability on a cold shock protein. Nat. Struct. Biol. 7:2000;380-383.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 380-383
    • Perl, D.1
  • 35
    • 0036136161 scopus 로고    scopus 로고
    • Removal of surface charge-charge interactions from ubiquitin leaves the protein folded and very stable
    • Loladze V.V., Makhatadze G.I. Removal of surface charge-charge interactions from ubiquitin leaves the protein folded and very stable. Protein Sci. 11:2002;174-177.
    • (2002) Protein Sci. , vol.11 , pp. 174-177
    • Loladze, V.V.1    Makhatadze, G.I.2
  • 36
    • 0028213362 scopus 로고
    • Protein stabilization by hydrophobic interactions at the surface
    • van den Burg B., et al. Protein stabilization by hydrophobic interactions at the surface. Eur. J. Biochem. 220:1994;981-985.
    • (1994) Eur. J. Biochem. , vol.220 , pp. 981-985
    • Van den Burg, B.1
  • 37
    • 0032032172 scopus 로고    scopus 로고
    • Surface-exposed phenylalanines in the RNP1/RNP2 motif stabilize the cold-shock protein CspB from Bacillus subtilis
    • Schindler T., et al. Surface-exposed phenylalanines in the RNP1/RNP2 motif stabilize the cold-shock protein CspB from Bacillus subtilis. Proteins. 30:1998;401-406.
    • (1998) Proteins , vol.30 , pp. 401-406
    • Schindler, T.1
  • 38
    • 0001843147 scopus 로고    scopus 로고
    • Coupling protein stability and protein function in Escherichia coli CspA
    • Hillier B.J., et al. Coupling protein stability and protein function in Escherichia coli CspA. Fold. Des. 3:1998;87-93.
    • (1998) Fold. Des. , vol.3 , pp. 87-93
    • Hillier, B.J.1
  • 39
    • 0028904906 scopus 로고
    • Hydrogen bonds and the pH dependence of ovomucoid third domain stability
    • Swint-Kruse L., Robertson A.D. Hydrogen bonds and the pH dependence of ovomucoid third domain stability. Biochemistry. 34:1995;4724-4732.
    • (1995) Biochemistry , vol.34 , pp. 4724-4732
    • Swint-Kruse, L.1    Robertson, A.D.2
  • 40
    • 0028983182 scopus 로고
    • A values of the denatured state are on average 0.4 units lower than those of model compounds
    • A values of the denatured state are on average 0.4 units lower than those of model compounds. Biochemistry. 34:1995;9424-9433.
    • (1995) Biochemistry , vol.34 , pp. 9424-9433
    • Oliveberg, M.1
  • 41
    • 0033551039 scopus 로고    scopus 로고
    • a values and the pH dependent stability of the N-terminal domain of L9 as probes of electrostatic interactions in the denatured state. Differentiation between local and nonlocal interactions
    • a values and the pH dependent stability of the N-terminal domain of L9 as probes of electrostatic interactions in the denatured state. Differentiation between local and nonlocal interactions. Biochemistry. 38:1999;4896-4903.
    • (1999) Biochemistry , vol.38 , pp. 4896-4903
    • Kuhlman, B.1
  • 42
    • 0032535188 scopus 로고    scopus 로고
    • Coulombic effects of remote subsites on the active site of ribonuclease A
    • Fisher B.M., et al. Coulombic effects of remote subsites on the active site of ribonuclease A. Biochemistry. 37:1998;17386-17401.
    • (1998) Biochemistry , vol.37 , pp. 17386-17401
    • Fisher, B.M.1
  • 43
    • 0035964164 scopus 로고    scopus 로고
    • Dissecting the electrostatic interactions and pH-dependent activity of a family 11 glycosidase
    • Joshi M.D., et al. Dissecting the electrostatic interactions and pH-dependent activity of a family 11 glycosidase. Biochemistry. 40:2001;10115-10139.
    • (2001) Biochemistry , vol.40 , pp. 10115-10139
    • Joshi, M.D.1
  • 44
    • 0033534526 scopus 로고    scopus 로고
    • RNA recognition by the human U1A protein is mediated by a network of local cooperative interactions that create the optimal binding surface
    • Kranz J.K., Hall K.B. RNA recognition by the human U1A protein is mediated by a network of local cooperative interactions that create the optimal binding surface. J. Mol. Biol. 285:1999;215-231.
    • (1999) J. Mol. Biol. , vol.285 , pp. 215-231
    • Kranz, J.K.1    Hall, K.B.2
  • 45
    • 0035919649 scopus 로고    scopus 로고
    • Covariance analysis of RNA recognition motifs identifies functionally linked amino acids
    • Crowder S., et al. Covariance analysis of RNA recognition motifs identifies functionally linked amino acids. J. Mol. Biol. 310:2001;793-800.
    • (2001) J. Mol. Biol. , vol.310 , pp. 793-800
    • Crowder, S.1
  • 46
    • 0032559428 scopus 로고    scopus 로고
    • RNA-binding mediates the local cooperativity between the β-sheet and the C-terminal tail of the human U1A RBD1 protein
    • Kranz J.K., Hall K.B. RNA-binding mediates the local cooperativity between the β-sheet and the C-terminal tail of the human U1A RBD1 protein. J. Mol. Biol. 275:1998;465-481.
    • (1998) J. Mol. Biol. , vol.275 , pp. 465-481
    • Kranz, J.K.1    Hall, K.B.2
  • 47
    • 0025126043 scopus 로고
    • Strategy for analysing the co-operativity of intramolecular interactions in peptides and proteins
    • Horovitz A., Fersht A.R. Strategy for analysing the co-operativity of intramolecular interactions in peptides and proteins. J. Mol. Biol. 214:1990;613-617.
    • (1990) J. Mol. Biol. , vol.214 , pp. 613-617
    • Horovitz, A.1    Fersht, A.R.2
  • 48
    • 0036681440 scopus 로고    scopus 로고
    • a values in proteins
    • a values in proteins. Proteins. 48:2002;388-403.
    • (2002) Proteins , vol.48 , pp. 388-403
    • Forsyth, W.R.1
  • 49
    • 0032789936 scopus 로고    scopus 로고
    • Electrostatic interactions in the GCN4 leucine zipper: Substantial contributions arise from intramolecular interactions enhanced on binding
    • Hendsch Z.S., Tidor B. Electrostatic interactions in the GCN4 leucine zipper: Substantial contributions arise from intramolecular interactions enhanced on binding. Protein Sci. 8:1999;1381-1392.
    • (1999) Protein Sci. , vol.8 , pp. 1381-1392
    • Hendsch, Z.S.1    Tidor, B.2
  • 50
    • 0031891022 scopus 로고    scopus 로고
    • Computation of electrostatic complements to proteins: A case of charge stabilized binding
    • Chong L.T., et al. Computation of electrostatic complements to proteins: A case of charge stabilized binding. Protein Sci. 7:1998;206-210.
    • (1998) Protein Sci. , vol.7 , pp. 206-210
    • Chong, L.T.1
  • 51
    • 0023034393 scopus 로고
    • The general control of amino acid biosynthetic genes in the yeast Saccharomyces cerevisiae
    • Hinnebusch A.G. The general control of amino acid biosynthetic genes in the yeast Saccharomyces cerevisiae. CRC Crit. Rev. Biochem. 21:1986;277-317.
    • (1986) CRC Crit. Rev. Biochem. , vol.21 , pp. 277-317
    • Hinnebusch, A.G.1
  • 52
    • 0023644679 scopus 로고
    • Structure of ubiquitin refined at 1.8 Å resolution
    • Vijay-Kumar S., et al. Structure of ubiquitin refined at 1.8 Å resolution. J. Mol. Biol. 194:1987;531-544.
    • (1987) J. Mol. Biol. , vol.194 , pp. 531-544
    • Vijay-Kumar, S.1
  • 53
    • 0028004607 scopus 로고
    • Crystal structure at 1.92 Å resolution of the RNA-binding domain of the U1A spliceosomal protein complexed with an RNA hairpin
    • Oubridge C., et al. Crystal structure at 1.92 Å resolution of the RNA-binding domain of the U1A spliceosomal protein complexed with an RNA hairpin. Nature. 372:1994;432-438.
    • (1994) Nature , vol.372 , pp. 432-438
    • Oubridge, C.1
  • 54
    • 0026331267 scopus 로고
    • X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil
    • O'Shea E.K., et al. X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil. Science. 254:1991;539-544.
    • (1991) Science , vol.254 , pp. 539-544
    • O'Shea, E.K.1


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