메뉴 건너뛰기




Volumn 77, Issue 4, 2009, Pages 812-822

Elucidating the exact role of engineered CRABPII residues for the formation of a retinal protonated Schiff base

Author keywords

B rgi Dunitz angle; Cellular retinoic acid binding protein; Ordered water network; Rhodopsin protein mimic; Schiff base

Indexed keywords

ARGININE; CELLULAR RETINOIC ACID BINDING PROTEIN 2; GLUTAMINE; IMINE; LYSINE; RETINAL; RETINOIC ACID BINDING PROTEIN; SCHIFF BASE; THREONINE; TYROSINE; UNCLASSIFIED DRUG;

EID: 70450085594     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22495     Document Type: Article
Times cited : (11)

References (50)
  • 1
    • 46449109015 scopus 로고    scopus 로고
    • Structure and energetics of the hydrogen-bonded backbone in protein folding
    • Bolen DW, Rose GD. Structure and energetics of the hydrogen-bonded backbone in protein folding. Annu Rev Biochem 2008;77:339-362.
    • (2008) Annu Rev Biochem , vol.77 , pp. 339-362
    • Bolen, D.W.1    Rose, G.D.2
  • 3
    • 0034846953 scopus 로고    scopus 로고
    • Functional and structural roles of constituent amino acid residues of bovine pancreatic ribonuclease a
    • DOI 10.1263/jbb.92.98
    • Chatani E, Hayashi R. Functional and structural roles of constituent amino acid residues of bovine pancreatic ribonuclease A. J Biosci Bioeng 2001;92:98-107. (Pubitemid 32846406)
    • (2001) Journal of Bioscience and Bioengineering , vol.92 , Issue.2 , pp. 98-107
    • Chatani, E.1    Hayashi, R.2
  • 5
    • 47749083052 scopus 로고    scopus 로고
    • From the first protein structures to our current knowledge of protein folding: Delights and scepticisms
    • Fersht AR. From the first protein structures to our current knowledge of protein folding: delights and scepticisms. Nat Rev Mol Cell Biol 2008;9:650-654.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 650-654
    • Fersht, A.R.1
  • 6
    • 9744226460 scopus 로고    scopus 로고
    • A twisted base? the role of arginine in enzyme-catalyzed proton abstractions
    • DOI 10.1016/j.abb.2004.09.018, PII S0003986104005326
    • Guillen Schlippe YV, Hedstrom L. A twisted base? The role of arginine in enzyme-catalyzed proton abstractions. Arch Biochem Biophys 2005;433:266-278. (Pubitemid 39586597)
    • (2005) Archives of Biochemistry and Biophysics , vol.433 , Issue.1 , pp. 266-278
    • Guillen Schlippe, Y.V.1    Hedstrom, L.2
  • 7
    • 47549096255 scopus 로고    scopus 로고
    • Modulation of allostery of pyruvate kinase by shifting of an ensemble of microstates
    • Lee JC. Modulation of allostery of pyruvate kinase by shifting of an ensemble of microstates. Acta Biochim Biophys Sinica 2008;40:663-669.
    • (2008) Acta Biochim Biophys Sinica , vol.40 , pp. 663-669
    • Lee, J.C.1
  • 8
    • 0036384350 scopus 로고    scopus 로고
    • One fold with many functions: The evolutionary relationships between TIM barrel families based on their sequences, structures and functions
    • Nagano N, Orengo CA, Thornton JM. One fold with many functions: the evolutionary relationships between TIM barrel families based on their sequences, structures and functions. J Mol Biol 2002;321:741-765.
    • (2002) J Mol Biol , vol.321 , pp. 741-765
    • Nagano, N.1    Orengo, C.A.2    Thornton, J.M.3
  • 9
    • 15444362906 scopus 로고    scopus 로고
    • Local conformational fluctuations can modulate the coupling between proton binding and global structural transitions in proteins
    • Whitten ST, Garcia-Moreno EB, Hilser VJ. Local conformational fluctuations can modulate the coupling between proton binding and global structural transitions in proteins. Proc Natl Acad Sci USA 2005;102:4282-4287.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 4282-4287
    • Whitten, S.T.1    Garcia-Moreno, E.B.2    Hilser, V.J.3
  • 10
    • 4644355496 scopus 로고    scopus 로고
    • Analysis of protein folding and function using backbone modified proteins
    • DOI 10.1016/j.bioorg.2004.06.011, PII S0045206804000549, Mechanic Enzymology
    • Yang XY, Wang M, Fitzgerald MC. Analysis of protein folding and function using backbone modified proteins. Bioorg Chem 2004;32:438-449. (Pubitemid 39277445)
    • (2004) Bioorganic Chemistry , vol.32 , Issue.5 , pp. 438-449
    • Yang, X.1    Wang, M.2    Fitzgerald, M.C.3
  • 11
    • 0025685315 scopus 로고
    • Retinoic Acid receptors and cellular retinoid binding-proteins.I. A systematic study of their differential pattern of transcription during mouse organogenesis
    • Dolle P, Ruberte E, Leroy P, Morrisskay G, Chambon P. Retinoic Acid receptors and cellular retinoid binding-proteins.I. A systematic study of their differential pattern of transcription during mouse organogenesis. Development 1990;110:1133-1151.
    • (1990) Development , vol.110 , pp. 1133-1151
    • Dolle, P.1    Ruberte, E.2    Leroy, P.3    Morrisskay, G.4    Chambon, P.5
  • 13
    • 0029839230 scopus 로고    scopus 로고
    • Retinoic acid biosynthesis and metabolism
    • Napoli JL. Retinoic acid biosynthesis and metabolism. FASEB J 1996;10:993-1001.
    • (1996) FASEB J , vol.10 , pp. 993-1001
    • Napoli, J.L.1
  • 14
    • 0032831815 scopus 로고    scopus 로고
    • Interactions of retinoid binding proteins and enzymes in retinoid metabolism
    • DOI 10.1016/S1388-1981(99)00117-1, PII S1388198199001171
    • Napoli JL. Interactions of retinoid binding proteins and enzymes in retinoid metabolism. Biochim Biophys Acta 1999;1440:139-162. (Pubitemid 29424180)
    • (1999) Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids , vol.1440 , Issue.2-3 , pp. 139-162
    • Napoli, J.L.1
  • 15
    • 0003035905 scopus 로고
    • Cellular retinoid binding proteins
    • Sporn MB, Roberts AB, DeWitt S, Goodman DS, editors. 2nd edition. New York: Raven Press
    • Ong DE, Newcomer ME, Chytil F. Cellular retinoid binding proteins. In: Sporn MB, Roberts AB, DeWitt S, Goodman DS, editors. The retinoids: Biology, Chemistry and Medicine, 2nd edition. New York: Raven Press; 1994. pp 283-318.
    • (1994) The Retinoids: Biology, Chemistry and Medicine , pp. 283-318
    • Ong, D.E.1    Newcomer, M.E.2    Chytil, F.3
  • 16
    • 0028774713 scopus 로고
    • Crystal structures of cellular retinoic acid binding proteins I and II in complex with all-trans-retinoic acid and a synthetic retinoid
    • Kleywegt GJ, Bergfors T, Senn H, Lemotte P, Gsell B, Shudo K, Jones TA. Crystal-structures of cellular retinoic acid-binding protein-I and protein-II in complex with all-trans-retinoic acid and a synthetic retinoid. Structure 1994;2:1241-1258. (Pubitemid 124001322)
    • (1994) Structure , vol.2 , Issue.12 , pp. 1241-1258
    • Kleywegt, G.J.1    Bergfors, T.2    Senn, H.3    Le Motte, P.4    Gsell, B.5    Shudo, K.6    Jones, T.A.7
  • 17
    • 33749258949 scopus 로고    scopus 로고
    • The Structure of Apo-wild-type Cellular Retinoic Acid Binding Protein II at 1.4 A and its Relationship to Ligand Binding and Nuclear Translocation
    • DOI 10.1016/j.jmb.2006.08.059, PII S0022283606011120
    • Vaezeslami S, Mathes E, Vasileiou C, Borhan B, Geiger JH. The structure of apo-wild-type cellular retinoic acid binding protein II at 1.4 A and its relationship to ligand binding and nuclear translocation. J Mol Biol 2006;363:687-701. (Pubitemid 44486222)
    • (2006) Journal of Molecular Biology , vol.363 , Issue.3 , pp. 687-701
    • Vaezeslami, S.1    Mathes, E.2    Vasileiou, C.3    Borhan, B.4    Geiger, J.H.5
  • 18
    • 0031036744 scopus 로고    scopus 로고
    • Structure-function relationships of cellular retinoic acid-binding proteins: Quantitative analysis of the ligand binding properties of the wild- Type proteins and site-directed mutants
    • DOI 10.1074/jbc.272.3.1541
    • Wang LC, Li Y, Yan HG. Structure-function relationships of cellular retinoic acid-binding proteins - quantitative analysis of the ligand binding properties of the wild-type proteins and site-directed mutants. J Biol Chem 1997;272:1541-1547. (Pubitemid 27043233)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.3 , pp. 1541-1547
    • Wang, L.1    Li, Y.2    Yan, H.3
  • 19
    • 56649123412 scopus 로고    scopus 로고
    • Structural analysis of site-directed mutants of cellular retinoic acid binding protein ii addresses the relationship between structural integrity and ligand binding
    • Vaezeslami S, Jia X, Vasileiou C, Borhan B, Geiger JH. structural analysis of site-directed mutants of cellular retinoic acid binding protein ii addresses the relationship between structural integrity and ligand binding. Acta Crystallogr Sect D 2008;64:1228-1239.
    • (2008) Acta Crystallogr Sect D , vol.64 , pp. 1228-1239
    • Vaezeslami, S.1    Jia, X.2    Vasileiou, C.3    Borhan, B.4    Geiger, J.H.5
  • 23
    • 0015136835 scopus 로고
    • Wavelength regulation in visual pigment chromophore. Large induced bathocromic shifts in retinol and related polyenes
    • Blatz PE, Baumgart N, Balasubramaniyan V, Balasubramaniyan P, Stedman E. Wavelength regulation in visual pigment chromophore. Large induced bathocromic shifts in retinol and related polyenes. Photochem Photobiol 1971;14:531-549.
    • (1971) Photochem Photobiol , vol.14 , pp. 531-549
    • Blatz, P.E.1    Baumgart, N.2    Balasubramaniyan, V.3    Balasubramaniyan, P.4    Stedman, E.5
  • 24
    • 0015762727 scopus 로고
    • Wavelength regulation in visual pigments
    • Blatz PE, Liebman PA. Wavelength regulation in visual pigments. Exp Eye Res 1973;17:573-580.
    • (1973) Exp Eye Res , vol.17 , pp. 573-580
    • Blatz, P.E.1    Liebman, P.A.2
  • 25
    • 0000559536 scopus 로고
    • a of the retinal protonated schiff-base in retinal proteins - A study with model compounds
    • a of the retinal protonated schiff-base in retinal proteins - a study with model compounds. J Am Chem Soc 1993;115:3772-3773.
    • (1993) J Am Chem Soc , vol.115 , pp. 3772-3773
    • Gat, Y.1    Sheves, M.2
  • 27
    • 0035923444 scopus 로고    scopus 로고
    • Wavelength dependent cis-trans isomerization in vision
    • Kim JE, Tauber MJ, Mathies RA. Wavelength dependent cis-trans isomerization in vision. Biochemistry 2001;40:13774-13778.
    • (2001) Biochemistry , vol.40 , pp. 13774-13778
    • Kim, J.E.1    Tauber, M.J.2    Mathies, R.A.3
  • 29
    • 0000562254 scopus 로고
    • The adaptation of visual pigments to the photic environment
    • Photochemistry of vision, Dartnall HJA editor, New York: Springer
    • Lythgoe JN. The adaptation of visual pigments to the photic environment. In Handbook of sensory physiology, Vol.7/1, Photochemistry of vision, Dartnall HJA editor, New York: Springer, 1972. pp 604-624.
    • (1972) Handbook of Sensory Physiology , vol.7 , Issue.1 , pp. 604-624
    • Lythgoe, J.N.1
  • 30
    • 0026602578 scopus 로고
    • Absorption-spectra of human cone pigments
    • Merbs SL, Nathans J. Absorption-spectra of human cone pigments. Nature 1992;356:433-435.
    • (1992) Nature , vol.356 , pp. 433-435
    • Merbs, S.L.1    Nathans, J.2
  • 31
    • 33847086348 scopus 로고
    • Opsin shifts in bovine rhodopsin and bacteriorhodopsin - Comparison of 2 external point-charge models
    • Motto MG, Sheves M, Tsujimoto K, Baloghnair V, Nakanishi K. Opsin shifts in bovine rhodopsin and bacteriorhodopsin - comparison of 2 external point-charge models. J Am Chem Soc 1980;102:7947-7949.
    • (1980) J Am Chem Soc , vol.102 , pp. 7947-7949
    • Motto, M.G.1    Sheves, M.2    Tsujimoto, K.3    Baloghnair, V.4    Nakanishi, K.5
  • 32
    • 0022695490 scopus 로고
    • Molecular genetics of human color vision: The genes encoding blue, green, and red pigments
    • Nathans J, Thomas D, Hogness DS. Molecular-genetics of human color-vision - the genes encoding blue, green, and red pigments. Science 1986;232:193-202. (Pubitemid 16046600)
    • (1986) Science , vol.232 , Issue.4747 , pp. 193-202
    • Nathans, J.1    Thomas, D.2    Hogness, D.S.3
  • 33
    • 0026352455 scopus 로고
    • Design, chemical synthesis, and expression of genes for the 3 human color-vision pigments
    • Oprian DD, Asenjo AB, Lee N, Pelletier SL. Design, chemical synthesis, and expression of genes for the 3 human color-vision pigments. Biochemistry 1991;30:11367-11372.
    • (1991) Biochemistry , vol.30 , pp. 11367-11372
    • Oprian, D.D.1    Asenjo, A.B.2    Lee, N.3    Pelletier, S.L.4
  • 34
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino-acid sequence data
    • Gill SC, Vonhippel PH. Calculation of protein extinction coefficients from amino-acid sequence data. Anal Biochem 1989;182:319-326.
    • (1989) Anal Biochem , vol.182 , pp. 319-326
    • Gill, S.C.1    Vonhippel, P.H.2
  • 35
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Otwinowski Z, Minor W. Processing of X-ray diffraction data collected in oscillation mode. Macromol Crystallogr A 1997;276:307-326. (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 36
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An Automated Program for Molecular Replacement
    • Vagin A, Teplyakov A. MOLREP: an automated program for molecular replacement. J Appl Crystallogr 1997;30:1022-1025. (Pubitemid 127485985)
    • (1997) Journal of Applied Crystallography , vol.30 , Issue.6 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 37
    • 0028103275 scopus 로고
    • The CCP4 Suite - Programs for protein crystallography
    • Bailey S. The CCP4 Suite - programs for protein crystallography. Acta Crystallogr Sect D 1994;50:760-763.
    • (1994) Acta Crystallogr Sect D , vol.50 , pp. 760-763
    • Bailey, S.1
  • 39
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov GN, Vagin AA, Dodson EJ. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr Sect D 1997;53:240-255.
    • (1997) Acta Crystallogr Sect D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 42
    • 0035182073 scopus 로고    scopus 로고
    • Use of TLS parameters to model anisotropic displacements in macromolecular refinement
    • Winn MD, Isupov MN, Murshudov GN. Use of TLS parameters to model anisotropic displacements in macromolecular refinement. Acta Crystallogr Sect D 2001;57:122-133.
    • (2001) Acta Crystallogr Sect D , vol.57 , pp. 122-133
    • Winn, M.D.1    Isupov, M.N.2    Murshudov, G.N.3
  • 43
    • 0033559918 scopus 로고    scopus 로고
    • Hydrogen bonding, hydrophobic interactions, and failure of the rigid receptor hypothesis
    • Davis AM, Teague SJ. Hydrogen bonding, hydrophobic interactions, and failure of the rigid receptor hypothesis. Angew Chem Int Ed 1999;38:737-749. (Pubitemid 129701960)
    • (1999) Angewandte Chemie - International Edition , vol.38 , Issue.6 , pp. 737-749
    • Davis, A.M.1    Teague, S.J.2
  • 44
    • 33751073728 scopus 로고    scopus 로고
    • Recognition forces in ligand-protein complexes: Blending information from different sources
    • DOI 10.1016/j.bcp.2006.05.022, PII S0006295206003248
    • Ermondi G, Caron G. Recognition forces in ligand-protein complexes: blending information from different sources. Biochem Pharmacol 2006;72:1633-1645. (Pubitemid 44764998)
    • (2006) Biochemical Pharmacology , vol.72 , Issue.12 , pp. 1633-1645
    • Ermondi, G.1    Caron, G.2
  • 46
    • 0022883904 scopus 로고
    • Alteration of pK(a) of the bacteriorhodopsin protonated Schiff base. a study with model compounds
    • DOI 10.1021/bi00366a040
    • Baasov T, Sheves M. Alteration of pKa of the bacteriorhodopsin protonated Schiff-base - a study with model compounds. Biochemistry 1986;25:5249-5258. (Pubitemid 17016539)
    • (1986) Biochemistry , vol.25 , Issue.18 , pp. 5249-5258
    • Baasov, T.1    Sheves, M.2
  • 48
    • 0026054732 scopus 로고
    • Effect of intermolecular orientation upon proton-transfer within a polarizable medium
    • Scheiner S, Duan XF. Effect of intermolecular orientation upon proton-transfer within a polarizable medium. Biophys J 1991;60:874-883.
    • (1991) Biophys J , vol.60 , pp. 874-883
    • Scheiner, S.1    Duan, X.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.