메뉴 건너뛰기




Volumn 20, Issue 4, 2007, Pages 253-262

The influence of rigid or flexible linkage between two ligands on the effective affinity and avidity for reversible interactions with bivalent receptors

Author keywords

Binding cooperativity; Bivalent avidity; Ligand receptor interaction; Local concentration; Monovalent affinity

Indexed keywords

CELL SURFACE RECEPTOR; LIGAND; PROTEIN SUBUNIT; RECOMBINANT PROTEIN;

EID: 34948842517     PISSN: 09523499     EISSN: 10991352     Source Type: Journal    
DOI: 10.1002/jmr.836     Document Type: Article
Times cited : (27)

References (29)
  • 1
    • 0029826479 scopus 로고    scopus 로고
    • The carboxyl terminus of the bacteriophage T4 DNA polymerase is required for holoenzyme complex formation
    • Berdis A, Soumillion P, Benkovic S. 1996. The carboxyl terminus of the bacteriophage T4 DNA polymerase is required for holoenzyme complex formation. Proc. Natl. Acad. Sci. USA 93: 12822-12827.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 12822-12827
    • Berdis, A.1    Soumillion, P.2    Benkovic, S.3
  • 2
    • 16244420152 scopus 로고    scopus 로고
    • Evaluation of intramolecular interaction between complementary domains, connected with a flexible chain
    • Bobrovnik SA, Stevens FJ. 2004. Evaluation of intramolecular interaction between complementary domains, connected with a flexible chain. Ukr. Zh. Biokhim. 76(6): 127-129.
    • (2004) Ukr. Zh. Biokhim , vol.76 , Issue.6 , pp. 127-129
    • Bobrovnik, S.A.1    Stevens, F.J.2
  • 3
    • 0015313012 scopus 로고
    • The influence of polyvalency on the binding properties of antibodies
    • Crothers DM, Metzger H. 1972. The influence of polyvalency on the binding properties of antibodies. Immunochemistry 9: 341-357.
    • (1972) Immunochemistry , vol.9 , pp. 341-357
    • Crothers, D.M.1    Metzger, H.2
  • 4
    • 0037168492 scopus 로고    scopus 로고
    • Effect of phosphorylation on the interdomain interaction of the response regulator, NarL
    • Eldridge AM, Kang H-S, Johnson E, Gunsalus R, Dahlquist FW. 2002. Effect of phosphorylation on the interdomain interaction of the response regulator, NarL. Biochemistry 41: 15173-15180.
    • (2002) Biochemistry , vol.41 , pp. 15173-15180
    • Eldridge, A.M.1    Kang, H.-S.2    Johnson, E.3    Gunsalus, R.4    Dahlquist, F.W.5
  • 5
    • 0000074776 scopus 로고
    • Statistical mechanics of wormlike chains. I. Asymptotic behavior
    • Gobush W, Yamawaka H, Stockmayer WH, Magee WS. 1972. Statistical mechanics of wormlike chains. I. Asymptotic behavior. J. Chem. Phys. 57: 2839-2843.
    • (1972) J. Chem. Phys , vol.57 , pp. 2839-2843
    • Gobush, W.1    Yamawaka, H.2    Stockmayer, W.H.3    Magee, W.S.4
  • 6
    • 0014488788 scopus 로고
    • The interaction of hapten-coupled bacteriophage phi-X-174 with antihapten antibody
    • Hornick CL, Karush F. 1969. The interaction of hapten-coupled bacteriophage phi-X-174 with antihapten antibody. Israel J. Med. Sci. 5: 163-170.
    • (1969) Israel J. Med. Sci , vol.5 , pp. 163-170
    • Hornick, C.L.1    Karush, F.2
  • 7
    • 0015315530 scopus 로고
    • Antibody affinity. 3. The role of multivalance
    • Hornick CL, Karush F. 1972. Antibody affinity. 3. The role of multivalance. Immunochemistry 9: 325-340.
    • (1972) Immunochemistry , vol.9 , pp. 325-340
    • Hornick, C.L.1    Karush, F.2
  • 8
    • 0019407381 scopus 로고
    • On the attribution and additivity of binding energies
    • Jencks WP. 1981. On the attribution and additivity of binding energies. Proc. Natl. Acad. Sci. U S A 78: 4046-4050.
    • (1981) Proc. Natl. Acad. Sci. U S A , vol.78 , pp. 4046-4050
    • Jencks, W.P.1
  • 10
    • 0026705890 scopus 로고
    • Effect of bivalent interaction upon apparent antibody affinity: Experimental confirmation of theory using fluorescence photobleaching and implications for antibody binding assays
    • Kaufman EN, Jain RK. 1992. Effect of bivalent interaction upon apparent antibody affinity: experimental confirmation of theory using fluorescence photobleaching and implications for antibody binding assays. Cancer Res. 52: 4157-4167.
    • (1992) Cancer Res , vol.52 , pp. 4157-4167
    • Kaufman, E.N.1    Jain, R.K.2
  • 11
    • 0032539902 scopus 로고    scopus 로고
    • Getting a handhold on DNA: Design of poly-zinc finger proteins with femtomolar dissociation constants
    • Kim J-S, Pabo CO. 1998. Getting a handhold on DNA: design of poly-zinc finger proteins with femtomolar dissociation constants. Proc. Natl. Acad. Sci. USA 95: 2812-2817.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 2812-2817
    • Kim, J.-S.1    Pabo, C.O.2
  • 12
    • 0035852693 scopus 로고    scopus 로고
    • Design of polyzinc finger peptides with structured linkers
    • Moore M, Choo Y, Klug A. 2001. Design of polyzinc finger peptides with structured linkers. Proc. Natl. Acad. Sci. USA 98: 1432-1436.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 1432-1436
    • Moore, M.1    Choo, Y.2    Klug, A.3
  • 13
    • 0022397326 scopus 로고
    • Dissociation of antibodies bound to surface-immobilized antigen
    • Nygren H, Czerkinsky C, Stenberg M. 1985. Dissociation of antibodies bound to surface-immobilized antigen. J. Immunol. Methods 85: 87-95.
    • (1985) J. Immunol. Methods , vol.85 , pp. 87-95
    • Nygren, H.1    Czerkinsky, C.2    Stenberg, M.3
  • 14
    • 0034923498 scopus 로고    scopus 로고
    • Design and selection of novel Cys2His2 zinc finger proteins
    • Pabo CO, Peisach E, Grant RA. 2001. Design and selection of novel Cys2His2 zinc finger proteins. Annu. Rev. Biochem. 70: 313-340.
    • (2001) Annu. Rev. Biochem , vol.70 , pp. 313-340
    • Pabo, C.O.1    Peisach, E.2    Grant, R.A.3
  • 15
    • 0025054642 scopus 로고
    • Binding of a monoclonal antibody and its Fab fragment to supported phospholipid monolayers measured by total internal reflection fluorescence microscopy
    • Pisarchick ML, Thompson NL. 1990. Binding of a monoclonal antibody and its Fab fragment to supported phospholipid monolayers measured by total internal reflection fluorescence microscopy. Biophys. J. 58: 1235-1249.
    • (1990) Biophys. J , vol.58 , pp. 1235-1249
    • Pisarchick, M.L.1    Thompson, N.L.2
  • 16
    • 0029671279 scopus 로고    scopus 로고
    • Covalent attachment of Arc repressor subunits by a peptide linker enhances affinity for operator DNA
    • Robinson CR, Sauer RT. 1996. Covalent attachment of Arc repressor subunits by a peptide linker enhances affinity for operator DNA. Biochemistry 35: 109-116.
    • (1996) Biochemistry , vol.35 , pp. 109-116
    • Robinson, C.R.1    Sauer, R.T.2
  • 17
    • 0030973043 scopus 로고    scopus 로고
    • Dual targets of a transcriptional activator that tracks on DNA
    • Sanders G, Kassavetis G, Geiduschek E. 1997. Dual targets of a transcriptional activator that tracks on DNA. EMBO J. 16: 3124-3132.
    • (1997) EMBO J , vol.16 , pp. 3124-3132
    • Sanders, G.1    Kassavetis, G.2    Geiduschek, E.3
  • 19
    • 4644292468 scopus 로고    scopus 로고
    • Arm-domain interactions can provide high binding cooperativity
    • Schleif R, Wolberger C. 2004. Arm-domain interactions can provide high binding cooperativity. Protein Sci. 13: 2829-2831.
    • (2004) Protein Sci , vol.13 , pp. 2829-2831
    • Schleif, R.1    Wolberger, C.2
  • 20
    • 0036163042 scopus 로고    scopus 로고
    • A conserved tetrapeptide motif: Potentiating apoptosis through IAP-binding
    • Shi Y. 2002. A conserved tetrapeptide motif: potentiating apoptosis through IAP-binding. Cell Death Differ. 9: 93-95.
    • (2002) Cell Death Differ , vol.9 , pp. 93-95
    • Shi, Y.1
  • 21
    • 3042610198 scopus 로고    scopus 로고
    • Biochemical and physiological properties of the DNA binding domain of AraC protein
    • Timmes A, Rodgers M, Schleif R. 2004. Biochemical and physiological properties of the DNA binding domain of AraC protein. J. Mol. Biol. 340: 731-738.
    • (2004) J. Mol. Biol , vol.340 , pp. 731-738
    • Timmes, A.1    Rodgers, M.2    Schleif, R.3
  • 22
    • 0348110323 scopus 로고    scopus 로고
    • Segmental flexibility and avidity of IgM in the interaction of polyvalent antigens
    • Tobita T, Oda M, Azuma T. 2004. Segmental flexibility and avidity of IgM in the interaction of polyvalent antigens. Molec. Immunol. 40: 803-811.
    • (2004) Molec. Immunol , vol.40 , pp. 803-811
    • Tobita, T.1    Oda, M.2    Azuma, T.3
  • 23
    • 0024227164 scopus 로고
    • Antibody multivalency effects in the direct binding model for vesicle immunolysis assays
    • Waite BA, Chang EL. 1988. Antibody multivalency effects in the direct binding model for vesicle immunolysis assays. J. Immunol. Methods 115: 227-238.
    • (1988) J. Immunol. Methods , vol.115 , pp. 227-238
    • Waite, B.A.1    Chang, E.L.2
  • 24
    • 0030245149 scopus 로고    scopus 로고
    • Radial distribution function of semiflexible polymers
    • Wilhelm J, Frey E. 1996. Radial distribution function of semiflexible polymers. Phys. Rev. Lett. 77: 2581-2584.
    • (1996) Phys. Rev. Lett , vol.77 , pp. 2581-2584
    • Wilhelm, J.1    Frey, E.2
  • 25
    • 0034661843 scopus 로고    scopus 로고
    • Combining structure-based design with phage display to create new Cys(2)His(2) zinc finger dimers
    • Wolfe A, Ramm EI, Pabo CO. 2000. Combining structure-based design with phage display to create new Cys(2)His(2) zinc finger dimers. Structure 8: 739-750.
    • (2000) Structure , vol.8 , pp. 739-750
    • Wolfe, A.1    Ramm, E.I.2    Pabo, C.O.3
  • 26
    • 36849102256 scopus 로고
    • Statistical mechanics of wormlike chains. II. Excluded volume effects
    • Yamawaka H, Stockmayer WH. 1972. Statistical mechanics of wormlike chains. II. Excluded volume effects. J. Chem. Phys. 57: 2843-2854.
    • (1972) J. Chem. Phys , vol.57 , pp. 2843-2854
    • Yamawaka, H.1    Stockmayer, W.H.2
  • 27
    • 0035909804 scopus 로고    scopus 로고
    • The affinity-enhancing roles of flexible linkers in two-domain DNA-binding proteins
    • Zhou H-X. 2001a. The affinity-enhancing roles of flexible linkers in two-domain DNA-binding proteins. Biochemistry 40: 15069-15073.
    • (2001) Biochemistry , vol.40 , pp. 15069-15073
    • Zhou, H.-X.1
  • 28
    • 0034804243 scopus 로고    scopus 로고
    • Single-chain versus dimeric protein folding: Thermodynamic and kinetic consequences of covalent linkage
    • Zhou H-X. 2001b. Single-chain versus dimeric protein folding: thermodynamic and kinetic consequences of covalent linkage. J. Am. Chem. Soc. 123: 6730-6731.
    • (2001) J. Am. Chem. Soc , vol.123 , pp. 6730-6731
    • Zhou, H.-X.1
  • 29
    • 0037540052 scopus 로고    scopus 로고
    • Quantitative account of the enhanced affinity of two linked scFvs specific for different epitopes on the same antigen
    • Zhou H-X. 2003. Quantitative account of the enhanced affinity of two linked scFvs specific for different epitopes on the same antigen. J. Mol. Biol. 329: 1-8.
    • (2003) J. Mol. Biol , vol.329 , pp. 1-8
    • Zhou, H.-X.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.