메뉴 건너뛰기




Volumn 65, Issue 5, 1997, Pages 609-630

Towards a molecular understanding of phase separation in the lens: A comparison of the X-ray structures of two high T(c) γ-crystallins, γE and γF, with two low T(c) γ-crystallins, γB and γD

Author keywords

amino aromatic interactions; dipole moment; eye lens; ion pairs; phase separation; X ray structure; crystallins

Indexed keywords

GAMMA CRYSTALLIN;

EID: 0030710251     PISSN: 00144835     EISSN: None     Source Type: Journal    
DOI: 10.1006/exer.1997.0368     Document Type: Article
Times cited : (44)

References (40)
  • 1
    • 0028289035 scopus 로고
    • Probing the microenvironments of tryptophan residues in the monomeric crystallins of the bovine lens
    • 96
    • Augusteyn, R. C. Chandresekher, G. Ghiggino, K. P. Vassett, P. 1994, Probing the microenvironments of tryptophan residues in the monomeric crystallins of the bovine lens. Biochim. Biophys. Acta, 1205, 89, 96.
    • (1994) Biochim. Biophys. Acta , vol.1205 , pp. 89
    • Augusteyn, R.C.1    Chandresekher, G.2    Ghiggino, K.P.3    Vassett, P.4
  • 4
    • 58149455081 scopus 로고
    • Studies onγ-crystallins from calf lens
    • 61
    • Björk, I. 1964, Studies onγ-crystallins from calf lens. Exp. Eye Res. 3, 254, 61.
    • (1964) Exp. Eye Res. , vol.3 , pp. 254
    • Björk, I.1
  • 8
    • 0023140814 scopus 로고
    • Crystallographic R-factor refinement by molecular-dynamics
    • 60
    • Brünger, A. T. Kuryan, J. Karplus, M. 1987, Crystallographic R-factor refinement by molecular-dynamics. Science, 235, 458, 60.
    • (1987) Science , vol.235 , pp. 458
    • Brünger, A.T.1    Kuryan, J.2    Karplus, M.3
  • 9
    • 0023139115 scopus 로고
    • Phase separation in lens cytoplasm is genetically linked to cataract formation in the Philly mouse
    • 5
    • Clark, J. I. Carper, D. 1987, Phase separation in lens cytoplasm is genetically linked to cataract formation in the Philly mouse. Proc. Natl. Acad. Sci. U.S.A. 84, 122, 5.
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 122
    • Clark, J.I.1    Carper, D.2
  • 11
    • 0028103275 scopus 로고
    • The CCP4 Suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4. 3
    • Collaborative Computational Project, Number 4. 1994, The CCP4 Suite: Programs for protein crystallography. Acta Cryst. D50, 760, 3.
    • (1994) Acta Cryst. , vol.D50 , pp. 760
  • 12
    • 0000568418 scopus 로고
    • RESTRAIN - Restrained structure factor least squares refinement program for macromolecular structures
    • 16
    • Driessen, H. P. C. Haneef, M. I. J. Harris, G. W. Howlin, B. 1989, RESTRAIN - Restrained structure factor least squares refinement program for macromolecular structures. J. Appl. Cryst. 22, 510, 16.
    • (1989) J. Appl. Cryst. , vol.22 , pp. 510
    • Driessen, H.P.C.1    Haneef, M.I.J.2    Harris, G.W.3    Howlin, B.4
  • 14
    • 0027609916 scopus 로고
    • SETOR: Hardware lighted three-dimensional solid model representations of macromolecules
    • 8
    • Evans, S. V. 1993, SETOR: Hardware lighted three-dimensional solid model representations of macromolecules. J. Mol. Graphics, 11, 134, 8.
    • (1993) J. Mol. Graphics , vol.11 , pp. 134
    • Evans, S.V.1
  • 16
    • 0028001569 scopus 로고
    • Expression of recombinant bovineγB-Crystallin,γC-Crystallin andγD-crystallin and correlation with native proteins
    • 84
    • Hay, R. E. Andley, U. P. Petrash, J. M. 1994, Expression of recombinant bovineγB-Crystallin,γC-Crystallin andγD-crystallin and correlation with native proteins. Exp. Eye Res. 58, 573, 84.
    • (1994) Exp. Eye Res. , vol.58 , pp. 573
    • Hay, R.E.1    Andley, U.P.2    Petrash, J.M.3
  • 17
    • 19244380437 scopus 로고
    • Cytoplasmic phase separation in formation of galactosemic cataract in lenses of young rats
    • 16
    • Ishimoto, C. Goalwin, P. W. Sun, S.-T. Nishio, I. Tanaka, T. 1979, Cytoplasmic phase separation in formation of galactosemic cataract in lenses of young rats. Proc. Natl. Acad. Sci. U.S.A. 76, 4414, 16.
    • (1979) Proc. Natl. Acad. Sci. U.S.A. , vol.76 , pp. 4414
    • Ishimoto, C.1    Goalwin, P.W.2    Sun, S.-T.3    Nishio, I.4    Tanaka, T.5
  • 18
    • 0030052290 scopus 로고    scopus 로고
    • Role of hydration and water structure in biological and colloidal interactions
    • 25
    • Israelachvili, J. Wennerstrom, H. 1996, Role of hydration and water structure in biological and colloidal interactions. Nature, 369, 219, 25.
    • (1996) Nature , vol.369 , pp. 219
    • Israelachvili, J.1    Wennerstrom, H.2
  • 19
    • 0000356656 scopus 로고
    • FRODO: A graphics model-building and refinement system for macromolecules
    • 72
    • Jones, T. A. 1978, FRODO: a graphics model-building and refinement system for macromolecules. J. Appl. Cryst. 11, 268, 72.
    • (1978) J. Appl. Cryst. , vol.11 , pp. 268
    • Jones, T.A.1
  • 20
    • 0039908862 scopus 로고
    • Electrospray ionisation mass spectrometry of lens crystallins: Verification and detection of errors in protein sequences of bovineγ-crystallins
    • 8
    • Kilby, G. W. Truscott, R. J. W. Aquilina, J. A. Shiel, M. M. Riley, M. L. Harding, J. J. 1995, Electrospray ionisation mass spectrometry of lens crystallins: verification and detection of errors in protein sequences of bovineγ-crystallins. Eur. J. Mass Spectrometry, 1, 203, 8.
    • (1995) Eur. J. Mass Spectrometry , vol.1 , pp. 203
    • Kilby, G.W.1    Truscott, R.J.W.2    Aquilina, J.A.3    Shiel, M.M.4    Riley, M.L.5    Harding, J.J.6
  • 21
    • 0030513191 scopus 로고    scopus 로고
    • An eye-lens protein-water structure: 1/2 Å resolution structure of γb-crystallin at 150 K
    • 22
    • Kumaraswamy, V. S. Lindley, P. F. Slingsby, C. Glover, I. D. 1996, An eye-lens protein-water structure: 1/2 Å resolution structure of γB-crystallin at 150 K. Acta Cryst. D52, 611, 22.
    • (1996) Acta Cryst. , vol.D52 , pp. 611
    • Kumaraswamy, V.S.1    Lindley, P.F.2    Slingsby, C.3    Glover, I.D.4
  • 22
    • 0000243829 scopus 로고
    • PROCHECK-A program to check the stereochemical quality of protein structures
    • 91
    • Laskowski, R. A. MacArthur, M. W. Moss, D. S. Thornton, J. M. 1993, PROCHECK-A program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26, 283, 91.
    • (1993) J. Appl. Cryst. , vol.26 , pp. 283
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 23
    • 0015222647 scopus 로고
    • The interpretation of protein structure: Estimation of static accessibility
    • 400
    • Lee, B. Richards, F. M. 1971, The interpretation of protein structure: estimation of static accessibility. J. Mol. Biol. 55, 379, 400.
    • (1971) J. Mol. Biol. , vol.55 , pp. 379
    • Lee, B.1    Richards, F.M.2
  • 25
    • 0028351165 scopus 로고
    • Contribution of Unusual Arginine-Arginine Short-Range Interactions to Stabilisation and Recognition in Proteins
    • 215
    • Magalhaes, A. Maigret, B. Hoflack, J. Gomes, J. N. F. Scheraga, H. A. 1994, Contribution of Unusual Arginine-Arginine Short-Range Interactions to Stabilisation and Recognition in Proteins. J. Prot. Chem. 13, 195, 215.
    • (1994) J. Prot. Chem. , vol.13 , pp. 195
    • Magalhaes, A.1    Maigret, B.2    Hoflack, J.3    Gomes, J.N.F.4    Scheraga, H.A.5
  • 26
    • 0000478452 scopus 로고    scopus 로고
    • A model of attractive interactions to account for fluid-fluid phase separation of protein solutions
    • 300
    • Malfois, M. Bonneté, F. Belloni, L. Tardieu, A. 1996, A model of attractive interactions to account for fluid-fluid phase separation of protein solutions. J. Chem. Phys. 105, 3290, 300.
    • (1996) J. Chem. Phys. , vol.105 , pp. 3290
    • Malfois, M.1    Bonneté, F.2    Belloni, L.3    Tardieu, A.4
  • 28
    • 0023389564 scopus 로고
    • γ-crystallins of the human eye lens: Expression analysis of five members of the gene family
    • 9
    • Meakin, S. O. Du, R. P. Tsui, L-C. Breitman, M. L. 1987, γ-crystallins of the human eye lens: expression analysis of five members of the gene family. Mol. Cell. Biol. 7, 2671, 9.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 2671
    • Meakin, S.O.1    Du, R.P.2    Tsui, L.-C.3    Breitman, M.L.4
  • 29
    • 0000732609 scopus 로고
    • GRASP - Graphical representation and analysis of surface properties
    • Nicholls, A. Bharadwaj, R. Honig, B. 1993, GRASP - Graphical representation and analysis of surface properties. Biophys. J. 64, 166.
    • (1993) Biophys. J. , vol.64 , pp. 166
    • Nicholls, A.1    Bharadwaj, R.2    Honig, B.3
  • 30
    • 0025904729 scopus 로고
    • Suppression of phase separation in solutions of bovineγIV-crystallin by polar modification of the sulfur-containing amino acids
    • 20
    • Pande, J. Berland, C. Broide, M. Ogun, O. Melhuish, J. Benedek, G. 1991, Suppression of phase separation in solutions of bovineγIV-crystallin by polar modification of the sulfur-containing amino acids. Proc. Natl. Acad. Sci. U.S.A. 88, 4916, 20.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 4916
    • Pande, J.1    Berland, C.2    Broide, M.3    Ogun, O.4    Melhuish, J.5    Benedek, G.6
  • 31
    • 0014527761 scopus 로고
    • Distribution of protein within the normal rat lens
    • 70
    • Philipson, B. 1969, Distribution of protein within the normal rat lens. Invest. Ophthalmol. 8, 258, 70.
    • (1969) Invest. Ophthalmol. , vol.8 , pp. 258
    • Philipson, B.1
  • 33
    • 0008679116 scopus 로고
    • Opacification ofγ-crystallin solutions from calf lens in relation to cold cataract formation
    • 5
    • Siezen, R. J. Fisch, M. R. Slingsby, C. Benedek, G. B. 1985, Opacification ofγ-crystallin solutions from calf lens in relation to cold cataract formation. Proc. Natl. Acad. Sci. U.S.A. 82, 1701, 5.
    • (1985) Proc. Natl. Acad. Sci. U.S.A. , vol.82 , pp. 1701
    • Siezen, R.J.1    Fisch, M.R.2    Slingsby, C.3    Benedek, G.B.4
  • 34
    • 0023200844 scopus 로고
    • Human lensγ-crystallins: isolation, identification and characterization of the expressed gene products
    • 92
    • Siezen, R. J. Thomson, J. A. Kaplan, E. D. Benedek, G. B. 1987, Human lensγ-crystallins: isolation, identification and characterization of the expressed gene products. Proc. Natl. Acad. Sci. U.S.A. 84, 6088, 92.
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 6088
    • Siezen, R.J.1    Thomson, J.A.2    Kaplan, E.D.3    Benedek, G.B.4
  • 35
    • 0023942003 scopus 로고
    • Rat lensγ-crystallins: Characterization of the six gene products and their spatial and temporal distribution resulting from differential synthesis
    • 90
    • Siezen, R. J. Wu, E. Kaplan, E. D. Thomson, J. A. Benedek, G. B. 1988, Rat lensγ-crystallins: characterization of the six gene products and their spatial and temporal distribution resulting from differential synthesis. J. Mol. Biol. 199, 475, 90.
    • (1988) J. Mol. Biol. , vol.199 , pp. 475
    • Siezen, R.J.1    Wu, E.2    Kaplan, E.D.3    Thomson, J.A.4    Benedek, G.B.5
  • 36
    • 0021055001 scopus 로고
    • Purification and crystallization of mammalian lensγ-crystallins
    • 30
    • Slingsby, C. Miller, L. R. 1983, Purification and crystallization of mammalian lensγ-crystallins. Exp. Eye Res. 37, 517, 30.
    • (1983) Exp. Eye Res. , vol.37 , pp. 517
    • Slingsby, C.1    Miller, L.R.2
  • 37
    • 0017701259 scopus 로고
    • Phase separation of a protein-water mixture in cold cataract in the young rat lens
    • 12
    • Tanaka, T. Ishimoto, C. Chylack, L. T. 1977, Phase separation of a protein-water mixture in cold cataract in the young rat lens. Science, 197, 1010, 12.
    • (1977) Science , vol.197 , pp. 1010
    • Tanaka, T.1    Ishimoto, C.2    Chylack, L.T.3
  • 38
    • 0026554096 scopus 로고
    • Protein interactions in the calf eye lens: Interactions betweenβ-crystallins are repulsive whereas inγ-crystallins they are attractive
    • 12
    • Tardieu, A. Veretout, I. F. Krop, B. Slingsby, C. 1992, Protein interactions in the calf eye lens: interactions betweenβ-crystallins are repulsive whereas inγ-crystallins they are attractive. Eur. Biophys. J. 21, 1, 12.
    • (1992) Eur. Biophys. J. , vol.21 , pp. 1
    • Tardieu, A.1    Veretout, I.F.2    Krop, B.3    Slingsby, C.4
  • 40
    • 0024309379 scopus 로고
    • Packing interactions in the eye lens. Structural analysis, internal symmetry and lattice interactions ofγIVa-crystallin
    • 35
    • White, H. E. Driessen, H. P. C. Slingsby, C. Moss, D. S. Lindley, P. F. 1989, Packing interactions in the eye lens. Structural analysis, internal symmetry and lattice interactions ofγIVa-crystallin. J. Mol. Biol. 207, 217, 35.
    • (1989) J. Mol. Biol. , vol.207 , pp. 217
    • White, H.E.1    Driessen, H.P.C.2    Slingsby, C.3    Moss, D.S.4    Lindley, P.F.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.