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Volumn 99, Issue 5, 2010, Pages 1596-1603

An unusual hydrophobic core confers extreme flexibility to HEAT repeat proteins

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SOLENOIDEA;

EID: 77956544822     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2010.06.032     Document Type: Article
Times cited : (59)

References (49)
  • 1
  • 2
    • 35548969906 scopus 로고    scopus 로고
    • Functional architecture of the retromer cargo-recognition complex
    • Hierro, A., A. L. Rojas., J. H. Hurley. 2007. Functional architecture of the retromer cargo-recognition complex. Nature. 449:1063-1067.
    • (2007) Nature , vol.449 , pp. 1063-1067
    • Hierro, A.1    Rojas, A.L.2    Hurley, J.H.3
  • 3
    • 33847176295 scopus 로고    scopus 로고
    • Molecular mechanism of the nuclear protein import cycle
    • Stewart, M. 2007. Molecular mechanism of the nuclear protein import cycle. Nat. Rev. Mol. Cell Biol. 8:195-208.
    • (2007) Nat. Rev. Mol. Cell. Biol. , vol.8 , pp. 195-208
    • Stewart, M.1
  • 4
    • 10344262047 scopus 로고    scopus 로고
    • Molecular model for a complete clathrin lattice from electron cryomicroscopy
    • Fotin, A., Y. Cheng., T. Walz. 2004. Molecular model for a complete clathrin lattice from electron cryomicroscopy. Nature. 432:573-579.
    • (2004) Nature , vol.432 , pp. 573-579
    • Fotin, A.1    Cheng, Y.2    Walz, T.3
  • 5
    • 69849083412 scopus 로고    scopus 로고
    • The nuclear pore complex has entered the atomic age
    • Brohawn, S. G., J. R. Partridge., T. U. Schwartz. 2009. The nuclear pore complex has entered the atomic age. Structure. 17:1156-1168.
    • (2009) Structure , vol.17 , pp. 1156-1168
    • Brohawn, S.G.1    Partridge, J.R.2    Schwartz, T.U.3
  • 6
    • 0034306119 scopus 로고    scopus 로고
    • When protein folding is simplified to protein coiling: The continuum of solenoid protein structures
    • Kobe, B., and A. V. Kajava. 2000. When protein folding is simplified to protein coiling: the continuum of solenoid protein structures. Trends Biochem. Sci. 25:509-515.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 509-515
    • Kobe, B.1    Kajava, A.V.2
  • 7
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: Re-assessing the protein structure-function paradigm
    • Wright, P. E., and H. J. Dyson. 1999. Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm. J. Mol. Biol. 293:321-331.
    • (1999) J. Mol. Biol. , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 8
    • 44649192390 scopus 로고    scopus 로고
    • Importin-β: Structural and dynamic determinants of a molecular spring
    • Zachariae, U., and H. Grubmüller. 2008. Importin-β: structural and dynamic determinants of a molecular spring. Structure. 16:906-915.
    • (2008) Structure , vol.16 , pp. 906-915
    • Zachariae, U.1    Grubmüller, H.2
  • 9
    • 0025212107 scopus 로고
    • Evidence for a molten globule state as a general intermediate in protein folding
    • Ptitsyn, O. B., R. H. Pain., O. I. Razgulyaev. 1990. Evidence for a molten globule state as a general intermediate in protein folding. FEBS Lett. 262:20-24.
    • (1990) FEBS Lett. , vol.262 , pp. 20-24
    • Ptitsyn, O.B.1    Pain, R.H.2    Razgulyaev, O.I.3
  • 10
    • 0028807509 scopus 로고
    • Inactivation precedes overall molecular conformation changes during enzyme denaturation
    • Tsou, C. L. 1995. Inactivation precedes overall molecular conformation changes during enzyme denaturation. Biochim. Biophys. Acta. 1253:151-162.
    • (1995) Biochim. Biophys. Acta , vol.1253 , pp. 151-162
    • Tsou, C.L.1
  • 11
    • 0029160445 scopus 로고
    • How the molten globule became
    • Ptitsyn, O. B. 1995. How the molten globule became. Trends Biochem. Sci. 20:376-379.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 376-379
    • Ptitsyn, O.B.1
  • 12
    • 4444260365 scopus 로고    scopus 로고
    • An enzymatic molten globule: Efficient coupling of folding and catalysis
    • Vamvaca, K., B. Vögeli., D. Hilvert. 2004. An enzymatic molten globule: efficient coupling of folding and catalysis. Proc. Natl. Acad. Sci. USA. 101:12860-12864.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 12860-12864
    • Vamvaca, K.1    Vögeli, B.2    Hilvert, D.3
  • 13
    • 44449087047 scopus 로고    scopus 로고
    • Single-molecule force spectroscopy: Optical tweezers, magnetic tweezers and atomic force microscopy
    • Neuman, K. C., and A. Nagy. 2008. Single-molecule force spectroscopy: optical tweezers, magnetic tweezers and atomic force microscopy. Nat. Methods. 5:491-505.
    • (2008) Nat. Methods , vol.5 , pp. 491-505
    • Neuman, K.C.1    Nagy, A.2
  • 14
    • 77950599892 scopus 로고    scopus 로고
    • Mechanical unfolding of an ankyrin repeat protein
    • Serquera, D., W. Lee., L. S. Itzhaki. 2010. Mechanical unfolding of an ankyrin repeat protein. Biophys. J. 98:1294-1301.
    • (2010) Biophys. J. , vol.98 , pp. 1294-1301
    • Serquera, D.1    Lee, W.2    Itzhaki, L.S.3
  • 15
    • 48249124180 scopus 로고    scopus 로고
    • Shifting transition states in the unfolding of a large ankyrin repeat protein
    • Werbeck, N. D., P. J. E. Rowling., L. S. Itzhaki. 2008. Shifting transition states in the unfolding of a large ankyrin repeat protein. Proc. Natl. Acad. Sci. USA. 105:9982-9987.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 9982-9987
    • Werbeck, N.D.1    Rowling, P.J.E.2    Itzhaki, L.S.3
  • 16
    • 0033582763 scopus 로고    scopus 로고
    • Single molecule force spectroscopy of spectrin repeats: Low unfolding forces in helix bundles
    • DOI 10.1006/jmbi.1998.2466
    • Rief, M., J. Pascual., H. E. Gaub. 1999. Single molecule force spectroscopy of spectrin repeats: low unfolding forces in helix bundles. J. Mol. Biol. 286:553-561. (Pubitemid 29090169)
    • (1999) Journal of Molecular Biology , vol.286 , Issue.2 , pp. 553-561
    • Rief, M.1    Pascual, J.2    Saraste, M.3    Gaub, H.E.4
  • 17
    • 33644849450 scopus 로고    scopus 로고
    • Nanospring behavior of ankyrin repeats
    • Lee, G., K. Abdi., P. E. Marszalek. 2006. Nanospring behavior of ankyrin repeats. Nature. 440:246-249.
    • (2006) Nature , vol.440 , pp. 246-249
    • Lee, G.1    Abdi, K.2    Marszalek, P.E.3
  • 18
    • 0029392854 scopus 로고
    • HEAT repeats in the Huntington's disease protein
    • Andrade, M. A., and P. Bork. 1995. HEAT repeats in the Huntington's disease protein. Nat. Genet. 11:115-116.
    • (1995) Nat. Genet. , vol.11 , pp. 115-116
    • Andrade, M.A.1    Bork, P.2
  • 19
    • 19444383899 scopus 로고    scopus 로고
    • Structural basis for the high-affinity binding of nucleoporin Nup1p to the Saccharomyces cerevisiae importin-β homologue, Kap95p
    • Liu, S. M., and M. Stewart. 2005. Structural basis for the high-affinity binding of nucleoporin Nup1p to the Saccharomyces cerevisiae importin-β homologue, Kap95p. J. Mol. Biol. 349:515-525.
    • (2005) J. Mol. Biol. , vol.349 , pp. 515-525
    • Liu, S.M.1    Stewart, M.2
  • 20
    • 33646482468 scopus 로고    scopus 로고
    • Karyopherin flexibility in nucleocytoplasmic transport
    • Conti, E., C. W. Müller, and M. Stewart. 2006. Karyopherin flexibility in nucleocytoplasmic transport. Curr. Opin. Struct. Biol. 16:237-244.
    • (2006) Curr. Opin. Struct. Biol. , vol.16 , pp. 237-244
    • Conti, E.1    Müller, C.W.2    Stewart, M.3
  • 21
    • 0033587167 scopus 로고    scopus 로고
    • Structure of importin-β bound to the IBB domain of importin-α
    • Cingolani, G., C. Petosa., C. W. Müller. 1999. Structure of importin-β bound to the IBB domain of importin-α. Nature. 399:221-229.
    • (1999) Nature , vol.399 , pp. 221-229
    • Cingolani, G.1    Petosa, C.2    Müller, C.W.3
  • 22
    • 20444468112 scopus 로고    scopus 로고
    • Structural basis for nuclear import complex dissociation by RanGTP
    • Lee, S. J., Y. Matsuura., M. Stewart. 2005. Structural basis for nuclear import complex dissociation by RanGTP. Nature. 435:693-696.
    • (2005) Nature , vol.435 , pp. 693-696
    • Lee, S.J.1    Matsuura, Y.2    Stewart, M.3
  • 24
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • Hess, B., C. Kutzner., E. Lindahl. 2008. GROMACS 4: algorithms for highly efficient, load-balanced, and scalable molecular simulation. J. Chem. Theory Comput. 4:435-447.
    • (2008) J. Chem. Theory Comput. , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Lindahl, E.3
  • 25
    • 33645941402 scopus 로고
    • The OPLS potential functions for proteins. Energy minimizations for crystals of cyclic-peptides and crambin
    • Jorgensen, W. L., and J. Tirado-Rives. 1988. The OPLS potential functions for proteins. Energy minimizations for crystals of cyclic-peptides and crambin. J. Am. Chem. Soc. 110:1657-1666.
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 1657-1666
    • Jorgensen, W.L.1    Tirado-Rives, J.2
  • 26
    • 0004016501 scopus 로고
    • Comparison of simple potential functions for simulating liquid water
    • Jorgensen, W. L., J. Chandrasekhar., M. L. Klein. 1983. Comparison of simple potential functions for simulating liquid water. J. Comput. Phys. 79:926-935.
    • (1983) J. Comput. Phys. , vol.79 , pp. 926-935
    • Jorgensen, W.L.1    Chandrasekhar, J.2    Klein, M.L.3
  • 27
    • 0000388705 scopus 로고    scopus 로고
    • LINCS: A linear constraint solver for molecular simulations
    • Hess, B., H. Bekker., J. G. E. M. Fraaije. 1997. LINCS: a linear constraint solver for molecular simulations. J. Comput. Chem. 18:1463-1472.
    • (1997) J. Comput. Chem. , vol.18 , pp. 1463-1472
    • Hess, B.1    Bekker, H.2    Fraaije, J.G.E.M.3
  • 28
    • 33750587438 scopus 로고
    • Molecular dynamics with coupling to an external bath
    • Berendsen, H. J. C., J. P. M. Postma., J. R. Haak. 1984. Molecular dynamics with coupling to an external bath. J. Chem. Phys. 81:3684-3690.
    • (1984) J. Chem. Phys. , vol.81 , pp. 3684-3690
    • Berendsen, H.J.C.1    Postma, J.P.M.2    Haak, J.R.3
  • 29
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An nlog (n) method for Ewald sums in large systems
    • Darden, T., D. York, and L. Pedersen. 1993. Particle mesh Ewald: an nlog (n) method for Ewald sums in large systems. J. Chem. Phys. 98:10089-10092.
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 30
    • 33645961739 scopus 로고
    • A smooth particle mesh Ewald potential
    • Essmann, U., L. Perera., L. G. Pedersen. 1995. A smooth particle mesh Ewald potential. J. Chem. Phys. 103:8577-8592.
    • (1995) J. Chem. Phys. , vol.103 , pp. 8577-8592
    • Essmann, U.1    Perera, L.2    Pedersen, L.G.3
  • 31
    • 0030059225 scopus 로고    scopus 로고
    • Ligand binding: Molecular mechanics calculation of the streptavidin-biotin rupture force
    • Grubmüller, H., B. Heymann, and P. Tavan. 1996. Ligand binding: molecular mechanics calculation of the streptavidin-biotin rupture force. Science. 271:997-999.
    • (1996) Science , vol.271 , pp. 997-999
    • Grubmüller, H.1    Heymann, B.2    Tavan, P.3
  • 32
    • 0030972502 scopus 로고    scopus 로고
    • Molecular dynamics simulations of Leu-encephalin in water and DMSO
    • van der Spoel, D., and H. J. C. Berendsen. 1997. Molecular dynamics simulations of Leu-encephalin in water and DMSO. Biophys. J. 72:2032-2041.
    • (1997) Biophys. J. , vol.72 , pp. 2032-2041
    • Van Der Spoel, D.1    Berendsen, H.J.C.2
  • 33
    • 33646719091 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity
    • Lipari, G., and A. Szabo. 1982. Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity. J. Am. Chem. Soc. 104:4546-4559.
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4546-4559
    • Lipari, G.1    Szabo, A.2
  • 34
    • 0001351515 scopus 로고
    • Estimation of absolute and relative entropies of macromolecules using the covariance matrix
    • Schlitter, J. 1993. Estimation of absolute and relative entropies of macromolecules using the covariance matrix. Chem. Phys. Lett. 6:617-621.
    • (1993) Chem. Phys. Lett. , vol.6 , pp. 617-621
    • Schlitter, J.1
  • 35
    • 0023645282 scopus 로고
    • Structure of the ColE1 Rop protein at 1.7 Å resolution
    • Banner, D. W., M. Kokkinidis, and D. Tsernoglou. 1987. Structure of the ColE1 Rop protein at 1.7 Å resolution. J. Mol. Biol. 196:657-675.
    • (1987) J. Mol. Biol. , vol.196 , pp. 657-675
    • Banner, D.W.1    Kokkinidis, M.2    Tsernoglou, D.3
  • 36
    • 33748305808 scopus 로고    scopus 로고
    • A highly strained nuclear conformation of the exportin Cse1p revealed by molecular dynamics simulations
    • Zachariae, U., and H. Grubmüller. 2006. A highly strained nuclear conformation of the exportin Cse1p revealed by molecular dynamics simulations. Structure. 14:1469-1478.
    • (2006) Structure , vol.14 , pp. 1469-1478
    • Zachariae, U.1    Grubmüller, H.2
  • 37
    • 17044401714 scopus 로고    scopus 로고
    • In search of the hair-cell gating spring elastic properties of ankyrin and cadherin repeats
    • Sotomayor, M., D. P. Corey, and K. Schulten. 2005. In search of the hair-cell gating spring elastic properties of ankyrin and cadherin repeats. Structure. 13:669-682.
    • (2005) Structure , vol.13 , pp. 669-682
    • Sotomayor, M.1    Corey, D.P.2    Schulten, K.3
  • 38
    • 77249156811 scopus 로고    scopus 로고
    • PR65, the HEAT-repeat scaffold of phosphatase PP2A, is an elastic connector that links force and catalysis
    • Grinthal, A., I. Adamovic., N. Kleckner. 2010. PR65, the HEAT-repeat scaffold of phosphatase PP2A, is an elastic connector that links force and catalysis. Proc. Natl. Acad. Sci. USA. 107:2467-2472.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 2467-2472
    • Grinthal, A.1    Adamovic, I.2    Kleckner, N.3
  • 40
    • 2442665377 scopus 로고    scopus 로고
    • Bacteriophage capsids: Tough nanoshells with complex elastic properties
    • Ivanovska, I. L., P. J. de Pablo., G. J. Wuite. 2004. Bacteriophage capsids: tough nanoshells with complex elastic properties. Proc. Natl. Acad. Sci. USA. 101:7600-7605.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 7600-7605
    • Ivanovska, I.L.1    De Pablo, P.J.2    Wuite, G.J.3
  • 41
    • 62649155309 scopus 로고    scopus 로고
    • Mechanical properties of the icosahedral shell of southern bean mosaic virus: A molecular dynamics study
    • Zink, M., and H. Grubmüller. 2009. Mechanical properties of the icosahedral shell of southern bean mosaic virus: a molecular dynamics study. Biophys. J. 96:1350-1363.
    • (2009) Biophys. J. , vol.96 , pp. 1350-1363
    • Zink, M.1    Grubmüller, H.2
  • 42
    • 0035946941 scopus 로고    scopus 로고
    • Comparison of ARM and HEAT protein repeats
    • Andrade, M. A., C. Petosa., P. Bork. 2001. Comparison of ARM and HEAT protein repeats. J. Mol. Biol. 309:1-18.
    • (2001) J. Mol. Biol. , vol.309 , pp. 1-18
    • Andrade, M.A.1    Petosa, C.2    Bork, P.3
  • 43
    • 0035667264 scopus 로고    scopus 로고
    • Four-helix bundle topology re-engineered: Monomeric Rop protein variants with different loop arrangements
    • Kresse, H. P., M. Czubayko., H. Bloecker. 2001. Four-helix bundle topology re-engineered: monomeric Rop protein variants with different loop arrangements. Protein Eng. 14:897-901.
    • (2001) Protein Eng. , vol.14 , pp. 897-901
    • Kresse, H.P.1    Czubayko, M.2    Bloecker, H.3
  • 44
    • 0030057864 scopus 로고    scopus 로고
    • What makes a protein a protein? Hydrophobic core designs that specify stability and structural properties
    • Munson, M., S. Balasubramanian., L. Regan. 1996. What makes a protein a protein? Hydrophobic core designs that specify stability and structural properties. Protein Sci. 5:1584-1593.
    • (1996) Protein Sci. , vol.5 , pp. 1584-1593
    • Munson, M.1    Balasubramanian, S.2    Regan, L.3
  • 45
    • 0034477023 scopus 로고    scopus 로고
    • Dramatic structural and thermodynamic consequences of repacking a protein's hydrophobic core
    • Willis, M. A., B. Bishop., A. T. Brunger. 2000. Dramatic structural and thermodynamic consequences of repacking a protein's hydrophobic core. Structure. 8:1319-1328.
    • (2000) Structure , vol.8 , pp. 1319-1328
    • Willis, M.A.1    Bishop, B.2    Brunger, A.T.3
  • 46
    • 69949105161 scopus 로고    scopus 로고
    • The rules of disorder or why disorder rules
    • Gsponer, J., and M. M. Babu. 2009. The rules of disorder or why disorder rules. Prog. Biophys. Mol. Biol. 99:94-103.
    • (2009) Prog. Biophys. Mol. Biol. , vol.99 , pp. 94-103
    • Gsponer, J.1    Babu, M.M.2
  • 47
    • 45849131354 scopus 로고    scopus 로고
    • Recognition dynamics up to microseconds revealed from an RDC-derived ubiquitin ensemble in solution
    • Lange, O. F., N. A. Lakomek., B. L. de Groot. 2008. Recognition dynamics up to microseconds revealed from an RDC-derived ubiquitin ensemble in solution. Science. 320:1471-1475.
    • (2008) Science , vol.320 , pp. 1471-1475
    • Lange, O.F.1    Lakomek, N.A.2    De Groot, B.L.3
  • 48
    • 43149121353 scopus 로고    scopus 로고
    • Molecular basis for the recognition of snurportin 1 by importin β
    • Mitrousis, G., A. S. Olia., G. Cingolani. 2008. Molecular basis for the recognition of snurportin 1 by importin β. J. Biol. Chem. 283:7877-7884.
    • (2008) J. Biol. Chem. , vol.283 , pp. 7877-7884
    • Mitrousis, G.1    Olia, A.S.2    Cingolani, G.3
  • 49
    • 77956515584 scopus 로고    scopus 로고
    • Crystal structure of importin-β and SREBP-2 complex
    • Lee, S. J., T. Sekimoto., Y. Yoneda. 2003. Crystal structure of importin-β and SREBP-2 complex. Science. 302:1513-1514.
    • (2003) Science , vol.302 , pp. 1513-1514
    • Lee, S.J.1    Sekimoto, T.2    Yoneda, Y.3


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