메뉴 건너뛰기




Volumn 36, Issue 2, 1999, Pages 147-156

The effect of inhibitor binding on the structural stability and cooperativity of the HIV-1 protease

Author keywords

Calorimetry; Cooperative interactions; HIV; Protease

Indexed keywords

N ACETYLPEPSTATIN; PROTEINASE; PROTEINASE INHIBITOR;

EID: 0033181015     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(19990801)36:2<147::AID-PROT2>3.0.CO;2-3     Document Type: Article
Times cited : (60)

References (40)
  • 1
    • 0030905238 scopus 로고    scopus 로고
    • Structure-based thermodynamic analysis of HIV-1 protease inhibitors
    • Bardi JS, Luque I, Freire E. Structure-based thermodynamic analysis of HIV-1 protease inhibitors. Biochemistry 1997;36:6588-6596.
    • (1997) Biochemistry , vol.36 , pp. 6588-6596
    • Bardi, J.S.1    Luque, I.2    Freire, E.3
  • 2
    • 0032574705 scopus 로고    scopus 로고
    • The molecular basis of resistance to HIV-1 protease inhibition: A plausible hypothesis
    • Luque I, Todd MJ, Gomez J, Semo N, Freire E. The molecular basis of resistance to HIV-1 protease inhibition: a plausible hypothesis. Biochemistry 1998;37:5791-5797.
    • (1998) Biochemistry , vol.37 , pp. 5791-5797
    • Luque, I.1    Todd, M.J.2    Gomez, J.3    Semo, N.4    Freire, E.5
  • 3
    • 0032561137 scopus 로고    scopus 로고
    • The structural stability of the HIV-1 protease
    • Todd M, Semo N, Freire E. The structural stability of the HIV-1 protease. J Mol Biol 1998;283:475-488.
    • (1998) J Mol Biol , vol.283 , pp. 475-488
    • Todd, M.1    Semo, N.2    Freire, E.3
  • 4
    • 0026344399 scopus 로고
    • The three-dimensional structure of the aspartyl protease from the HIV-1 isolate BRU
    • Spinelli S, Liu QZ, Alzari PM, Hirel PH, Poljak RJ. The three-dimensional structure of the aspartyl protease from the HIV-1 isolate BRU. Biochimie 1991;73:1391-1396.
    • (1991) Biochimie , vol.73 , pp. 1391-1396
    • Spinelli, S.1    Liu, Q.Z.2    Alzari, P.M.3    Hirel, P.H.4    Poljak, R.J.5
  • 5
    • 0026009213 scopus 로고
    • Stable submolecular folding units in a non-compact form of cytochrome c
    • Jeng M-F, Englander SW. Stable submolecular folding units in a non-compact form of cytochrome c. J Mol Biol 1991;221:1045-1061.
    • (1991) J Mol Biol , vol.221 , pp. 1045-1061
    • Jeng, M.-F.1    Englander, S.W.2
  • 6
    • 0026731991 scopus 로고
    • Hydrogen exchange in native and denatured states of hen egg-white lysozyme
    • Radford SE, Buck M, Topping KD, Dobson CM, Evans PA. Hydrogen exchange in native and denatured states of hen egg-white lysozyme. Proteins 1992;14:237-248.
    • (1992) Proteins , vol.14 , pp. 237-248
    • Radford, S.E.1    Buck, M.2    Topping, K.D.3    Dobson, C.M.4    Evans, P.A.5
  • 7
    • 0027384196 scopus 로고
    • Hydrogen exchange in unligated and ligated staphylococcal nuclease
    • Loh SN, Prehoda KE, Wang J, Markley JL. Hydrogen exchange in unligated and ligated staphylococcal nuclease. Biochemistry 1993; 32:11022-11028.
    • (1993) Biochemistry , vol.32 , pp. 11022-11028
    • Loh, S.N.1    Prehoda, K.E.2    Wang, J.3    Markley, J.L.4
  • 8
    • 0027375522 scopus 로고
    • Protein internal flexibility and global stability: Effect of urea on hydrogen exchange rates of bovine pancreatic trypsin inhibitor
    • Kim K-S, Woodward C. Protein internal flexibility and global stability: Effect of urea on hydrogen exchange rates of bovine pancreatic trypsin inhibitor. Biochemistry 1993;32:9609-9613.
    • (1993) Biochemistry , vol.32 , pp. 9609-9613
    • Kim, K.-S.1    Woodward, C.2
  • 9
    • 0027361710 scopus 로고
    • Is the slow-exchange core the protein folding core?
    • Woodward C. Is the slow-exchange core the protein folding core? TIBS. 1993;18:359-360.
    • (1993) TIBS , vol.18 , pp. 359-360
    • Woodward, C.1
  • 10
    • 0030334648 scopus 로고    scopus 로고
    • An evaluation of the use of hydrogen exchange at equilibrium to probe intermediates on the folding pathway
    • Clarke J, Fersht AR. An evaluation of the use of hydrogen exchange at equilibrium to probe intermediates on the folding pathway. Folding Design 1996;1:243-254.
    • (1996) Folding Design , vol.1 , pp. 243-254
    • Clarke, J.1    Fersht, A.R.2
  • 11
    • 0030047378 scopus 로고    scopus 로고
    • Temperature and pH dependences of hydrogen exchange and global stability for ovomucoid third domain
    • Swint-Kruse L, Robertson AD. Temperature and pH dependences of hydrogen exchange and global stability for ovomucoid third domain. Biochemistry. 1996;35:171-180.
    • (1996) Biochemistry , vol.35 , pp. 171-180
    • Swint-Kruse, L.1    Robertson, A.D.2
  • 12
    • 0029643523 scopus 로고
    • Protein folding intermediates: Native-state hydrogen exchange
    • Bai Y, Sosnick TR, Mayne L, Englander SW. Protein folding intermediates: native-state hydrogen exchange. Science. 1995;269: 192-197.
    • (1995) Science , vol.269 , pp. 192-197
    • Bai, Y.1    Sosnick, T.R.2    Mayne, L.3    Englander, S.W.4
  • 13
    • 0028008617 scopus 로고
    • Staphylococcal nuclease folding intermediate charaterized by hydrogen exchange and NMR spectroscopy
    • Jacobs MD, Fox RO. Staphylococcal nuclease folding intermediate charaterized by hydrogen exchange and NMR spectroscopy. Proc Natl Acad Sci USA 1994;91:449-453.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 449-453
    • Jacobs, M.D.1    Fox, R.O.2
  • 15
    • 0028866620 scopus 로고
    • Different subdomains are most protected from hydrogen exchange in the molten globule and native states of human α-lactalbumin
    • Schulman BA, Redfield C, Peng Z, Dobson CM, Kim PS. Different subdomains are most protected from hydrogen exchange in the molten globule and native states of human α-lactalbumin. J Mol Biol 1995;253:651-657.
    • (1995) J Mol Biol , vol.253 , pp. 651-657
    • Schulman, B.A.1    Redfield, C.2    Peng, Z.3    Dobson, C.M.4    Kim, P.S.5
  • 16
    • 0032544060 scopus 로고    scopus 로고
    • The structural distribution of cooperative interactions in proteins: Analysis of the native state ensemble
    • Hilser VJ, Dowdy D, Oas TG, Freire E. The structural distribution of cooperative interactions in proteins: analysis of the native state ensemble. Proc Natl Acad Sci USA 1998;95:9903-9908.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 9903-9908
    • Hilser, V.J.1    Dowdy, D.2    Oas, T.G.3    Freire, E.4
  • 17
    • 0027245801 scopus 로고
    • Thermodynamic characterization of the structural stability of the coiled-coil region of the bZIP transcription factor GCN4
    • Thompson K, Vinson C, Freire E. Thermodynamic characterization of the structural stability of the coiled-coil region of the bZIP transcription factor GCN4. Biochemistry 1993;32:5491-5496.
    • (1993) Biochemistry , vol.32 , pp. 5491-5496
    • Thompson, K.1    Vinson, C.2    Freire, E.3
  • 18
    • 0000465244 scopus 로고    scopus 로고
    • Structural stability of oligomeric proteins
    • Johnson CR, Freire E. Structural stability of oligomeric proteins. Techniques Protein Chem 1996;VII:459-467.
    • (1996) Techniques Protein Chem , vol.7 , pp. 459-467
    • Johnson, C.R.1    Freire, E.2
  • 20
    • 0026734102 scopus 로고
    • Two-dimensional differential scanning calorimetry: Simultaneous resolution of intrinsic protein structural energetics and ligan binding interactions by global linkage analysis
    • Straume M, Freire E. Two-dimensional differential scanning calorimetry: simultaneous resolution of intrinsic protein structural energetics and ligan binding interactions by global linkage analysis. Anal Biochem 1992;203:259-268.
    • (1992) Anal Biochem , vol.203 , pp. 259-268
    • Straume, M.1    Freire, E.2
  • 21
    • 0000103534 scopus 로고
    • Statistical thermodynamic analysis of the heat capacity function associated with protein folding-unfolding transitions
    • Freire E. Statistical thermodynamic analysis of the heat capacity function associated with protein folding-unfolding transitions. Comments Mol Cell Biophys 1989;6:123-140.
    • (1989) Comments Mol Cell Biophys , vol.6 , pp. 123-140
    • Freire, E.1
  • 22
    • 0029080864 scopus 로고
    • Thermodynamic mapping of the inhibitor site of the aspartic protease endothiapepsin
    • Gomez J, Freire E. Thermodynamic mapping of the inhibitor site of the aspartic protease endothiapepsin. J Mol Biol 1995;252:337-350.
    • (1995) J Mol Biol , vol.252 , pp. 337-350
    • Gomez, J.1    Freire, E.2
  • 23
    • 0025281866 scopus 로고
    • Study of strong to ultralight protein interactions using differential scanning calorimetry
    • Brandts JF, Lin LN. Study of strong to ultralight protein interactions using differential scanning calorimetry. Biochemistry 1990; 29:6927-6940.
    • (1990) Biochemistry , vol.29 , pp. 6927-6940
    • Brandts, J.F.1    Lin, L.N.2
  • 24
    • 0026756702 scopus 로고
    • Thermodynamics of structural stability and cooperative folding behavior in proteins
    • Murphy KP, Freire E. Thermodynamics of structural stability and cooperative folding behavior in proteins. Adv Protein Chem 1992; 43:313-361.
    • (1992) Adv Protein Chem , vol.43 , pp. 313-361
    • Murphy, Kp.1    Freire, E.2
  • 26
    • 0029957505 scopus 로고    scopus 로고
    • The enthalpy change in protein folding and binding, refinement of parameters for structure based calculations
    • Hilser VJ, Gomez J, Freire E. The enthalpy change in protein folding and binding, refinement of parameters for structure based calculations. Proteins 1996;26:123-133.
    • (1996) Proteins , vol.26 , pp. 123-133
    • Hilser, V.J.1    Gomez, J.2    Freire, E.3
  • 27
    • 0027991081 scopus 로고
    • Estimation of changes in side chain configurational entropy in binding and folding: General methods and application to helix formation
    • Lee KH, Xie D, Freire E, Amzel LM. Estimation of changes in side chain configurational entropy in binding and folding: general methods and application to helix formation. Proteins 1994;20: 68-84.
    • (1994) Proteins , vol.20 , pp. 68-84
    • Lee, K.H.1    Xie, D.2    Freire, E.3    Amzel, L.M.4
  • 28
    • 0029900846 scopus 로고    scopus 로고
    • The magnitude of the backbone conformational entropy change in protein folding
    • DAquino JA et al. The magnitude of the backbone conformational entropy change in protein folding. Proteins. 1996;25:143-156.
    • (1996) Proteins , vol.25 , pp. 143-156
    • DAquino, J.A.1
  • 29
    • 0029958659 scopus 로고    scopus 로고
    • Structure based thermodynamic scale of α-helix propensities in amino acids
    • Luque I, Mayorga O, Freire E. Structure based thermodynamic scale of α-helix propensities in amino acids. Biochemistry 1996;35: 13681-13688.
    • (1996) Biochemistry , vol.35 , pp. 13681-13688
    • Luque, I.1    Mayorga, O.2    Freire, E.3
  • 30
    • 0026787837 scopus 로고
    • Use of protein unfolding studies to determine the conformational and dimeric stabilities of HIV-1 and SIV proteases
    • Grant SK et al. Use of protein unfolding studies to determine the conformational and dimeric stabilities of HIV-1 and SIV proteases. Biochemistry 1992;31:9491-9501.
    • (1992) Biochemistry , vol.31 , pp. 9491-9501
    • Grant, S.K.1
  • 31
    • 0030580089 scopus 로고    scopus 로고
    • Structure based calculation of the equilibrium folding pathway of proteins. Correlation with hydrogen exchange protection factors
    • Hilser VJ, Freire E. Structure based calculation of the equilibrium folding pathway of proteins. Correlation with hydrogen exchange protection factors. J Mol Biol 1996;262:756-772.
    • (1996) J Mol Biol , vol.262 , pp. 756-772
    • Hilser, V.J.1    Freire, E.2
  • 32
    • 0029968247 scopus 로고    scopus 로고
    • Global changes in amide hydrogen exchange rates for a protein antigen in complex with three different antibodies
    • Williams DC, Benjamin DC, Poljak RJ, Rule GS. Global changes in amide hydrogen exchange rates for a protein antigen in complex with three different antibodies. J Mol Biol 1996;257:866-876.
    • (1996) J Mol Biol , vol.257 , pp. 866-876
    • Williams, D.C.1    Benjamin, D.C.2    Poljak, R.J.3    Rule, G.S.4
  • 33
    • 0031746754 scopus 로고    scopus 로고
    • The statistical thermodynamic linkage between conformational and binding equilibrium
    • Freire E. The statistical thermodynamic linkage between conformational and binding equilibrium. Adv Protein Chem 1998;51:255-279.
    • (1998) Adv Protein Chem , vol.51 , pp. 255-279
    • Freire, E.1
  • 34
    • 0030993784 scopus 로고    scopus 로고
    • Structure-based statistical thermodynamic analysis of t4 lysozyme mutants: Structural mapping of cooperative interactions
    • Hilser VJ, Townsend BD, Freire E. Structure-based statistical thermodynamic analysis of t4 lysozyme mutants: structural mapping of cooperative interactions. Biophysical Chem. 1997;64: 69-79.
    • (1997) Biophysical Chem. , vol.64 , pp. 69-79
    • Hilser, V.J.1    Townsend, B.D.2    Freire, E.3
  • 35
    • 0031042186 scopus 로고    scopus 로고
    • Predicting the equilibrium protein folding pathway: Structure-based analysis of staphylococcal nuclease
    • Hilser VJ, Freire E. Predicting the equilibrium protein folding pathway: structure-based analysis of staphylococcal nuclease. Proteins. 1997;27:171-183.
    • (1997) Proteins , vol.27 , pp. 171-183
    • Hilser, V.J.1    Freire, E.2
  • 36
    • 0028921302 scopus 로고
    • Flexibility and function in HIV-1 protease
    • Nicholson LK et al. Flexibility and function in HIV-1 protease. Nat Struct Biol 1995;2:274-280.
    • (1995) Nat Struct Biol , vol.2 , pp. 274-280
    • Nicholson, L.K.1
  • 37
    • 0028845120 scopus 로고
    • Precise scanning calorimeter for studying thermal properties of biological macromolecules in dilute solution
    • Privalov G, Kavina V, Freire E, Privalov PL. Precise scanning calorimeter for studying thermal properties of biological macromolecules in dilute solution. Anal Biochem 1995;232:79-85.
    • (1995) Anal Biochem , vol.232 , pp. 79-85
    • Privalov, G.1    Kavina, V.2    Freire, E.3    Privalov, P.L.4
  • 39
    • 0000732609 scopus 로고
    • GRASP: Graphical representation and analysis of surface properties
    • Nicholls A, Bharadwaj R, Honig B. GRASP: graphical representation and analysis of surface properties. Biophys J 1993;64:166-170.
    • (1993) Biophys J , vol.64 , pp. 166-170
    • Nicholls, A.1    Bharadwaj, R.2    Honig, B.3
  • 40
    • 0028105957 scopus 로고
    • The HIV-1 protease as enzyme and substrate: Mutagenesis of autolysis sites and generation of a stable mutant with retained kinetic properties
    • Mildner AM, Rothrock DJ, Leone JW et al. The HIV-1 protease as enzyme and substrate: mutagenesis of autolysis sites and generation of a stable mutant with retained kinetic properties. Biochemistry 1994;33:9405-9413.
    • (1994) Biochemistry , vol.33 , pp. 9405-9413
    • Mildner, A.M.1    Rothrock, D.J.2    Leone, J.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.