메뉴 건너뛰기




Volumn 375, Issue 1, 2008, Pages 102-118

The Partly Folded Back Solution Structure Arrangement of the 30 SCR Domains in Human Complement Receptor Type 1 (CR1) Permits Access to its C3b and C4b Ligands

Author keywords

constrained modelling; molecular graphics; SCR domain; ultracentrifugation; X ray scattering

Indexed keywords

CLASSICAL COMPLEMENT PATHWAY C3 C5 CONVERTASE; COMPLEMENT COMPONENT C3B; COMPLEMENT COMPONENT C3B RECEPTOR; COMPLEMENT COMPONENT C4B; MEMBRANE PROTEIN;

EID: 36348990790     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.09.085     Document Type: Article
Times cited : (34)

References (55)
  • 2
    • 0035018479 scopus 로고    scopus 로고
    • Structure-function relationships of complement receptor type 1
    • Krych-Goldberg M., and Atkinson J.P. Structure-function relationships of complement receptor type 1. Immunol. Rev. 180 (2001) 112-122
    • (2001) Immunol. Rev. , vol.180 , pp. 112-122
    • Krych-Goldberg, M.1    Atkinson, J.P.2
  • 3
    • 0025354456 scopus 로고
    • Soluble human complement receptor type 1: in vivo inhibitor of complement suppressing post-ischemic myocardial inflammation and necrosis
    • Weisman H.F., Bartow T., Leppo M.K., Marsh Jr. H.C., Carson G.R., Concino M.F., et al. Soluble human complement receptor type 1: in vivo inhibitor of complement suppressing post-ischemic myocardial inflammation and necrosis. Science 249 (1990) 146-151
    • (1990) Science , vol.249 , pp. 146-151
    • Weisman, H.F.1    Bartow, T.2    Leppo, M.K.3    Marsh Jr., H.C.4    Carson, G.R.5    Concino, M.F.6
  • 4
    • 29744434976 scopus 로고    scopus 로고
    • Complement control protein modules in the regulators of complement activators
    • Morikis D., and Lambris J.D. (Eds), Taylor & Francis, Boca Raton, USA
    • Soares D., and Barlow P.N. Complement control protein modules in the regulators of complement activators. In: Morikis D., and Lambris J.D. (Eds). Structural Biology of the Complement System (2005), Taylor & Francis, Boca Raton, USA 19-62
    • (2005) Structural Biology of the Complement System , pp. 19-62
    • Soares, D.1    Barlow, P.N.2
  • 5
    • 33847237272 scopus 로고    scopus 로고
    • The interactive factor H-atypical hemolytic uremic syndrome mutation database and website: update and integration of membrane cofactor protein and Factor I mutations with structural models
    • Saunders R.E., Abarrategui-Garrido C., Fremeaux-Bacchi V., Goicoechea de Jorge E., Goodship T.H., Lopez Trascasa M., et al. The interactive factor H-atypical hemolytic uremic syndrome mutation database and website: update and integration of membrane cofactor protein and Factor I mutations with structural models. Hum. Mutat. 28 (2007) 222-234
    • (2007) Hum. Mutat. , vol.28 , pp. 222-234
    • Saunders, R.E.1    Abarrategui-Garrido, C.2    Fremeaux-Bacchi, V.3    Goicoechea de Jorge, E.4    Goodship, T.H.5    Lopez Trascasa, M.6
  • 6
    • 0027425977 scopus 로고
    • Structure of the gene for the F allele of complement receptor type 1 and sequence of the coding region unique to the S allele
    • Vik D.P., and Wong W.W. Structure of the gene for the F allele of complement receptor type 1 and sequence of the coding region unique to the S allele. J. Immunol. 151 (1993) 6214-6224
    • (1993) J. Immunol. , vol.151 , pp. 6214-6224
    • Vik, D.P.1    Wong, W.W.2
  • 7
    • 0037155690 scopus 로고    scopus 로고
    • Structure of the C3b binding site of CR1 (CD35), the immune adherence receptor
    • Smith B.O., Mallin R.L., Krych-Goldberg M., Wang X., Hauhart R.E., Bromek K., et al. Structure of the C3b binding site of CR1 (CD35), the immune adherence receptor. Cell 108 (2002) 769-780
    • (2002) Cell , vol.108 , pp. 769-780
    • Smith, B.O.1    Mallin, R.L.2    Krych-Goldberg, M.3    Wang, X.4    Hauhart, R.E.5    Bromek, K.6
  • 8
    • 11144357078 scopus 로고    scopus 로고
    • Backbone dynamics of complement control protein (CCP) modules reveals mobility in binding surfaces
    • O'Leary J.M., Bromek K., Black G.M., Uhrinova S., Schmitz C., Wang X., et al. Backbone dynamics of complement control protein (CCP) modules reveals mobility in binding surfaces. Protein Sci. 13 (2004) 1238-1250
    • (2004) Protein Sci. , vol.13 , pp. 1238-1250
    • O'Leary, J.M.1    Bromek, K.2    Black, G.M.3    Uhrinova, S.4    Schmitz, C.5    Wang, X.6
  • 9
    • 0036863301 scopus 로고    scopus 로고
    • Solution structures of complement components by X-ray and neutron scattering and analytical ultracentrifugation
    • Perkins S.J., Gilbert H.E., Aslam M., Hannan J.P., Holers V.M., and Goodship T.H.J. Solution structures of complement components by X-ray and neutron scattering and analytical ultracentrifugation. Biochem. Soc. Transt. 30 (2002) 996-1001
    • (2002) Biochem. Soc. Transt. , vol.30 , pp. 996-1001
    • Perkins, S.J.1    Gilbert, H.E.2    Aslam, M.3    Hannan, J.P.4    Holers, V.M.5    Goodship, T.H.J.6
  • 10
    • 33947609864 scopus 로고    scopus 로고
    • Relating small angle scattering and analytical ultracentrifugation in multidomain proteins
    • Scott D.J., Harding S.E., and Rowe A.J. (Eds), Royal Society of Chemistry, London, UK chapt. 15
    • Perkins S.J., Gilbert H.E., Lee Y.C., Sun Z., and Furtado P.B. Relating small angle scattering and analytical ultracentrifugation in multidomain proteins. In: Scott D.J., Harding S.E., and Rowe A.J. (Eds). Modern Analytical Ultracentrifugation: Techniques and Methods (2005), Royal Society of Chemistry, London, UK chapt. 15
    • (2005) Modern Analytical Ultracentrifugation: Techniques and Methods
    • Perkins, S.J.1    Gilbert, H.E.2    Lee, Y.C.3    Sun, Z.4    Furtado, P.B.5
  • 11
    • 35448974807 scopus 로고    scopus 로고
    • X-ray and neutron scattering data and their constrained molecular modelling
    • Correia J.J., and Dietrich III H.W. (Eds), Academic Press, San Diego
    • Perkins S.J., Okemefuna A.I., Fernando A.N., Bonner A., Gilbert H.E., and Furtado P.B. X-ray and neutron scattering data and their constrained molecular modelling. In: Correia J.J., and Dietrich III H.W. (Eds). Biophysical Tools for Biologists (2007), Academic Press, San Diego 375-423
    • (2007) Biophysical Tools for Biologists , pp. 375-423
    • Perkins, S.J.1    Okemefuna, A.I.2    Fernando, A.N.3    Bonner, A.4    Gilbert, H.E.5    Furtado, P.B.6
  • 12
    • 0035933335 scopus 로고    scopus 로고
    • Folded-back solution structure of monomeric factor H of human complement by synchrotron X-ray and neutron scattering, analytical ultracentrifugation and constrained molecular modelling
    • Aslam M., and Perkins S.J. Folded-back solution structure of monomeric factor H of human complement by synchrotron X-ray and neutron scattering, analytical ultracentrifugation and constrained molecular modelling. J. Mol. Biol. 309 (2001) 1117-1138
    • (2001) J. Mol. Biol. , vol.309 , pp. 1117-1138
    • Aslam, M.1    Perkins, S.J.2
  • 13
    • 33748440940 scopus 로고    scopus 로고
    • The 15 SCR domain structure of human complement receptor type 2 is semi-extended and flexible in solution: implications for function
    • Gilbert H.E., Asokan R., Holers V.M., and Perkins S.J. The 15 SCR domain structure of human complement receptor type 2 is semi-extended and flexible in solution: implications for function. J. Mol. Biol. 362 (2006) 1132-1147
    • (2006) J. Mol. Biol. , vol.362 , pp. 1132-1147
    • Gilbert, H.E.1    Asokan, R.2    Holers, V.M.3    Perkins, S.J.4
  • 14
    • 0037954130 scopus 로고    scopus 로고
    • The extended multidomain solution structures of the complement protein Crry and its chimaeric conjugate Crry-Ig by scattering, analytical ultracentrifugation and constrained modelling: implications for function and therapy
    • Aslam M., Guthridge J.M., Hack B.K., Quigg R.J., Holers V.M., and Perkins S.J. The extended multidomain solution structures of the complement protein Crry and its chimaeric conjugate Crry-Ig by scattering, analytical ultracentrifugation and constrained modelling: implications for function and therapy. J. Mol. Biol. 329 (2003) 525-550
    • (2003) J. Mol. Biol. , vol.329 , pp. 525-550
    • Aslam, M.1    Guthridge, J.M.2    Hack, B.K.3    Quigg, R.J.4    Holers, V.M.5    Perkins, S.J.6
  • 15
    • 13844266308 scopus 로고    scopus 로고
    • Solution structure of the complex between CR2 SCR 1-2 and C3d of human complement: an X-ray scattering and sedimentation modelling study
    • Gilbert H.E., Eaton J.T., Hannan J.P., Holers V.M., and Perkins S.J. Solution structure of the complex between CR2 SCR 1-2 and C3d of human complement: an X-ray scattering and sedimentation modelling study. J. Mol. Biol. 346 (2005) 859-873
    • (2005) J. Mol. Biol. , vol.346 , pp. 859-873
    • Gilbert, H.E.1    Eaton, J.T.2    Hannan, J.P.3    Holers, V.M.4    Perkins, S.J.5
  • 16
    • 33947593444 scopus 로고    scopus 로고
    • Associative and structural properties of the region of complement factor H encompassing the Tyr402His disease-related polymorphism and its interactions with heparin
    • Fernando A.N., Furtado P.B., Clark S.J., Gilbert H. E., Day A.J., Sim R.B., and Perkins S.J. Associative and structural properties of the region of complement factor H encompassing the Tyr402His disease-related polymorphism and its interactions with heparin. J. Mol. Biol. 368 (2007) 564-581
    • (2007) J. Mol. Biol. , vol.368 , pp. 564-581
    • Fernando, A.N.1    Furtado, P.B.2    Clark, S.J.3    Gilbert, H. E.4    Day, A.J.5    Sim, R.B.6    Perkins, S.J.7
  • 17
    • 36349016373 scopus 로고    scopus 로고
    • The regulatory SCR-1/5 and cell-surface-binding SCR-16/20 fragments of factor H reveal partially folded-back solution structures and different self-associative properties
    • Okemefuna A.I., Gilbert H.E., Griggs K.M., Ormsby R.J., Gordon D.L., and Perkins S.J. The regulatory SCR-1/5 and cell-surface-binding SCR-16/20 fragments of factor H reveal partially folded-back solution structures and different self-associative properties. J. Mol. Biol. 375 (2008) 80-101
    • (2008) J. Mol. Biol. , vol.375 , pp. 80-101
    • Okemefuna, A.I.1    Gilbert, H.E.2    Griggs, K.M.3    Ormsby, R.J.4    Gordon, D.L.5    Perkins, S.J.6
  • 18
    • 0024159572 scopus 로고
    • C5 convertase of the alternative complement pathway: covalent linkage between two C3b molecules within the trimolecular complex enzyme
    • Kinoshita T., Takata Y., Kozono H., Takeda J., Hong K.S., and Inoue K. C5 convertase of the alternative complement pathway: covalent linkage between two C3b molecules within the trimolecular complex enzyme. J. Immunol. 141 (1988) 3895-3901
    • (1988) J. Immunol. , vol.141 , pp. 3895-3901
    • Kinoshita, T.1    Takata, Y.2    Kozono, H.3    Takeda, J.4    Hong, K.S.5    Inoue, K.6
  • 19
    • 0023195099 scopus 로고
    • Covalent association of C3b with C4b within C5 convertase of the classical complement pathway
    • Takata Y., Kinoshita T., Kozono H., Takeda J., Tanaka E., Hong K., and Inoue K. Covalent association of C3b with C4b within C5 convertase of the classical complement pathway. J. Exp. Med. 165 (1987) 1494-1507
    • (1987) J. Exp. Med. , vol.165 , pp. 1494-1507
    • Takata, Y.1    Kinoshita, T.2    Kozono, H.3    Takeda, J.4    Tanaka, E.5    Hong, K.6    Inoue, K.7
  • 20
    • 0026498279 scopus 로고
    • Cell surface expression of the C3b/C4b receptor (CR1) protects Chinese hamster ovary cells from lysis by human complement
    • Makrides S.C., Scesney S.M., Ford P.J., Evans K.S., Carson G.R., and Marsh Jr. H.C. Cell surface expression of the C3b/C4b receptor (CR1) protects Chinese hamster ovary cells from lysis by human complement. J. Biol. Chem. 267 (1992) 24754-24761
    • (1992) J. Biol. Chem. , vol.267 , pp. 24754-24761
    • Makrides, S.C.1    Scesney, S.M.2    Ford, P.J.3    Evans, K.S.4    Carson, G.R.5    Marsh Jr., H.C.6
  • 21
    • 0028229875 scopus 로고
    • Quantitative analysis of C4b dimer binding to distinct sites on the C3b/C4b receptor (CR1)
    • Reilly B.D., Makrides S.C., Ford P.J., Marsh Jr. H.C., and Mold C. Quantitative analysis of C4b dimer binding to distinct sites on the C3b/C4b receptor (CR1). J. Biol. Chem. 269 (1994) 7696-7701
    • (1994) J. Biol. Chem. , vol.269 , pp. 7696-7701
    • Reilly, B.D.1    Makrides, S.C.2    Ford, P.J.3    Marsh Jr., H.C.4    Mold, C.5
  • 22
    • 25644452794 scopus 로고    scopus 로고
    • Structures of complement component C3 provide insights into the function and evolution of immunity
    • Janssen B.H., Huizinga E.G., Raaijmakers H.C., Roos A., Daha M.R., Nilsoon-Ekdahl K.K., et al. Structures of complement component C3 provide insights into the function and evolution of immunity. Nature 437 (2005) 505-511
    • (2005) Nature , vol.437 , pp. 505-511
    • Janssen, B.H.1    Huizinga, E.G.2    Raaijmakers, H.C.3    Roos, A.4    Daha, M.R.5    Nilsoon-Ekdahl, K.K.6
  • 23
    • 33750859976 scopus 로고    scopus 로고
    • Structure of C3b reveals conformation changes that underlie complement activity
    • Janssen B.J., Christodoulidou A., McCarthy A., Lambris J.D., and Gros P. Structure of C3b reveals conformation changes that underlie complement activity. Nature 444 (2006) 213-216
    • (2006) Nature , vol.444 , pp. 213-216
    • Janssen, B.J.1    Christodoulidou, A.2    McCarthy, A.3    Lambris, J.D.4    Gros, P.5
  • 26
    • 33750873601 scopus 로고    scopus 로고
    • Structure of C3b in complex with CRIg gives insights into regulation of complement activation
    • Wiesmann C., Katschke K.J., Yin J., Helmy K.Y., Steffek M., Fairbrother W.J., et al. Structure of C3b in complex with CRIg gives insights into regulation of complement activation. Nature 444 (2006) 217-220
    • (2006) Nature , vol.444 , pp. 217-220
    • Wiesmann, C.1    Katschke, K.J.2    Yin, J.3    Helmy, K.Y.4    Steffek, M.5    Fairbrother, W.J.6
  • 27
    • 0042855798 scopus 로고    scopus 로고
    • On the analysis of protein self-association by sedimentation velocity analytical ultracentrifugation
    • Schuck P. On the analysis of protein self-association by sedimentation velocity analytical ultracentrifugation. Anal. Biochem. 320 (2003) 104-124
    • (2003) Anal. Biochem. , vol.320 , pp. 104-124
    • Schuck, P.1
  • 28
    • 33745216899 scopus 로고    scopus 로고
    • Improved methods for fitting sedimentation coefficient distributions derived by time-derivative techniques
    • Philo J.S. Improved methods for fitting sedimentation coefficient distributions derived by time-derivative techniques. Anal. Biochem. 354 (2006) 238-246
    • (2006) Anal. Biochem. , vol.354 , pp. 238-246
    • Philo, J.S.1
  • 29
    • 0031688168 scopus 로고    scopus 로고
    • Sedimentation analysis of non-interacting and self-associating solutes using numerical solutions to the Lamm equation
    • Schuck P. Sedimentation analysis of non-interacting and self-associating solutes using numerical solutions to the Lamm equation. Biophys. J. 75 (1998) 1503-1512
    • (1998) Biophys. J. , vol.75 , pp. 1503-1512
    • Schuck, P.1
  • 30
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling
    • Schuck P. Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling. Biophys. J. 78 (2000) 1606-1619
    • (2000) Biophys. J. , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 31
    • 29944439131 scopus 로고    scopus 로고
    • An interactive web database of Factor H-associated haemolytic uremic syndrome mutations: insights into the structural consequences of disease-associated mutations
    • Saunders R.E., Goodship T.H.J., Zipfel P.E., and Perkins S.J. An interactive web database of Factor H-associated haemolytic uremic syndrome mutations: insights into the structural consequences of disease-associated mutations. Hum. Mutat. 27 (2006) 21-30
    • (2006) Hum. Mutat. , vol.27 , pp. 21-30
    • Saunders, R.E.1    Goodship, T.H.J.2    Zipfel, P.E.3    Perkins, S.J.4
  • 33
    • 0023049757 scopus 로고
    • Molecular modelling of human complement component C3 and its fragments by solution scattering
    • Perkins S.J., and Sim R.B. Molecular modelling of human complement component C3 and its fragments by solution scattering. Eur. J. Biochem. 157 (1986) 155-168
    • (1986) Eur. J. Biochem. , vol.157 , pp. 155-168
    • Perkins, S.J.1    Sim, R.B.2
  • 36
    • 0023049766 scopus 로고
    • Protein volumes and hydration effects: the calculation of partial specific volumes, neutron scattering matchpoints and 280 nm absorption coefficients for proteins and glycoproteins from amino acid sequences
    • Perkins S.J. Protein volumes and hydration effects: the calculation of partial specific volumes, neutron scattering matchpoints and 280 nm absorption coefficients for proteins and glycoproteins from amino acid sequences. Eur. J. Biochem. 157 (1986) 169-180
    • (1986) Eur. J. Biochem. , vol.157 , pp. 169-180
    • Perkins, S.J.1
  • 38
    • 0027576642 scopus 로고
    • X-ray powder diffraction analysis of silver behenate, a possible low-angle diffraction standard
    • Huang T.C., Toraya H., Blanton T.N., and Wu Y. X-ray powder diffraction analysis of silver behenate, a possible low-angle diffraction standard. J. Appl. Crystallog. 26 (1993) 180-184
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 180-184
    • Huang, T.C.1    Toraya, H.2    Blanton, T.N.3    Wu, Y.4
  • 39
    • 2142643646 scopus 로고    scopus 로고
    • Solution structure determination of monomeric human IgA2 by X-ray and neutron scattering, analytical ultracentrifugation and constrained modelling: a comparison with monomeric human IgA1
    • Furtado P.B., Whitty P.W., Robertson A., Eaton J.T., Almogren A., Kerr M.A., et al. Solution structure determination of monomeric human IgA2 by X-ray and neutron scattering, analytical ultracentrifugation and constrained modelling: a comparison with monomeric human IgA1. J. Mol. Biol. 338 (2004) 921-941
    • (2004) J. Mol. Biol. , vol.338 , pp. 921-941
    • Furtado, P.B.1    Whitty, P.W.2    Robertson, A.3    Eaton, J.T.4    Almogren, A.5    Kerr, M.A.6
  • 41
    • 0000980676 scopus 로고
    • X-ray small angle scattering with substances of biological interest in diluted solutions
    • Kratky O. X-ray small angle scattering with substances of biological interest in diluted solutions. Progr. Biophys. Chem. 13 (1963) 105-173
    • (1963) Progr. Biophys. Chem. , vol.13 , pp. 105-173
    • Kratky, O.1
  • 42
    • 0015891931 scopus 로고
    • Shape and volume of anti-poly(D-alanyl) antibodies in the presence and absence of tetra-D-alanine as followed by small-angle X-ray scattering
    • Pilz I., Kratky O., Licht A., and Sela M. Shape and volume of anti-poly(D-alanyl) antibodies in the presence and absence of tetra-D-alanine as followed by small-angle X-ray scattering. Biochemistry 12 (1973) 4998-5005
    • (1973) Biochemistry , vol.12 , pp. 4998-5005
    • Pilz, I.1    Kratky, O.2    Licht, A.3    Sela, M.4
  • 43
    • 0000634927 scopus 로고
    • Unusual ultrastructure of complement component C4b-binding protein of human complement by synchrotron X-ray scattering and hydrodynamic analysis
    • Perkins S.J., Chung L.P., and Reid K.B.M. Unusual ultrastructure of complement component C4b-binding protein of human complement by synchrotron X-ray scattering and hydrodynamic analysis. Biochem. J. 223 (1986) 779-807
    • (1986) Biochem. J. , vol.223 , pp. 779-807
    • Perkins, S.J.1    Chung, L.P.2    Reid, K.B.M.3
  • 44
    • 0026244044 scopus 로고
    • GNOM - a program package for small-angle scattering data-processing
    • Semenyuk A.V., and Svergun D.I. GNOM - a program package for small-angle scattering data-processing. J. Appl. Crystallog. 24 (1991) 537-540
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 537-540
    • Semenyuk, A.V.1    Svergun, D.I.2
  • 45
    • 0002498995 scopus 로고
    • Computer-aided interpretation of analytical sedimentation data for proteins
    • Harding S.E., Rowe A.J., and Horton J.C. (Eds), The Royal Society of Chemistry, Cambridge, UK
    • Laue T.M., Shah B.D., Ridgeway T.M., and Pelletier S. L. Computer-aided interpretation of analytical sedimentation data for proteins. In: Harding S.E., Rowe A.J., and Horton J.C. (Eds). Analytical Ultracentrifugation in Biochemistry and Polymer Science (1992), The Royal Society of Chemistry, Cambridge, UK 90-125
    • (1992) Analytical Ultracentrifugation in Biochemistry and Polymer Science , pp. 90-125
    • Laue, T.M.1    Shah, B.D.2    Ridgeway, T.M.3    Pelletier, S. L.4
  • 46
    • 0034654352 scopus 로고    scopus 로고
    • A method for directly fitting the time derivative of sedimentation velocity data and an alternative algorithm for calculating sedimentation coefficient distribution functions
    • Philo J. A method for directly fitting the time derivative of sedimentation velocity data and an alternative algorithm for calculating sedimentation coefficient distribution functions. Anal. Biochem. 279 (2000) 151-163
    • (2000) Anal. Biochem. , vol.279 , pp. 151-163
    • Philo, J.1
  • 47
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A., and Blundell T.L. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234 (1993) 779-815
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 48
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W., and Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22 (1983) 2577-2637
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 49
    • 0033548612 scopus 로고    scopus 로고
    • The Fab and Fc fragments of IgA1 exhibit a different arrangement from that in IgG: a study by X-ray and neutron solution scattering and homology modelling
    • Boehm M.K., Woof J.M., Kerr M.A., and Perkins S.J. The Fab and Fc fragments of IgA1 exhibit a different arrangement from that in IgG: a study by X-ray and neutron solution scattering and homology modelling. J. Mol. Biol. 286 (1999) 1421-1447
    • (1999) J. Mol. Biol. , vol.286 , pp. 1421-1447
    • Boehm, M.K.1    Woof, J.M.2    Kerr, M.A.3    Perkins, S.J.4
  • 50
    • 0035965873 scopus 로고    scopus 로고
    • X-ray and neutron scattering analyses of hydration shells: a molecular interpretation based on sequence predictions and modelling fits
    • Perkins S.J. X-ray and neutron scattering analyses of hydration shells: a molecular interpretation based on sequence predictions and modelling fits. Biophys. Chem. 93 (2001) 129-139
    • (2001) Biophys. Chem. , vol.93 , pp. 129-139
    • Perkins, S.J.1
  • 51
    • 0031587295 scopus 로고    scopus 로고
    • Pentameric and decameric structures in solution of the serum amyloid P component by X-ray and neutron scattering and molecular modelling analyses
    • Ashton A.W., Boehm M.K., Gallimore J.R., Pepys M.B., and Perkins S.J. Pentameric and decameric structures in solution of the serum amyloid P component by X-ray and neutron scattering and molecular modelling analyses. J. Mol. Biol. 272 (1997) 408-422
    • (1997) J. Mol. Biol. , vol.272 , pp. 408-422
    • Ashton, A.W.1    Boehm, M.K.2    Gallimore, J.R.3    Pepys, M.B.4    Perkins, S.J.5
  • 52
    • 0021112502 scopus 로고
    • Low resolution structural studies of mitochondrial ubiquinol-cytochrome c reductase in detergent solutions by neutron scattering
    • Perkins S.J., and Weiss H. Low resolution structural studies of mitochondrial ubiquinol-cytochrome c reductase in detergent solutions by neutron scattering. J. Mol. Biol. 168 (1983) 847-866
    • (1983) J. Mol. Biol. , vol.168 , pp. 847-866
    • Perkins, S.J.1    Weiss, H.2
  • 53
    • 0028828789 scopus 로고
    • Bent domain structure of recombinant human IgE-Fc in solution by X-ray and neutron scattering in conjunction with an automated curve fitting procedure
    • Beavil A.J., Young R.J., Sutton B.J., and Perkins S.J. Bent domain structure of recombinant human IgE-Fc in solution by X-ray and neutron scattering in conjunction with an automated curve fitting procedure. Biochemistry 34 (1995) 14449-14461
    • (1995) Biochemistry , vol.34 , pp. 14449-14461
    • Beavil, A.J.1    Young, R.J.2    Sutton, B.J.3    Perkins, S.J.4
  • 54
  • 55
    • 0001229341 scopus 로고    scopus 로고
    • Calculation of hydrodynamic properties of globular proteins from their atomic-level structure
    • Garcia de la Torre J., Huertas M.L., and Carrasco B. Calculation of hydrodynamic properties of globular proteins from their atomic-level structure. Biophys. J. 78 (2000) 719-730
    • (2000) Biophys. J. , vol.78 , pp. 719-730
    • Garcia de la Torre, J.1    Huertas, M.L.2    Carrasco, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.