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Volumn 337, Issue 4, 2004, Pages 893-903

Crystal structure of HEL4, a soluble, refoldable human VH single domain with a germ-line scaffold

Author keywords

Antibody; CDR, complementarity determining regions; Crystal structure; dAb, domain antibody; Folding; HEL, hen egg lysozyme; Human VH; Kd , dissociation constant; Mr , molecular mass; Single domain

Indexed keywords

FIBRIN; GLYCINE; MONOMER;

EID: 1642364974     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.02.013     Document Type: Article
Times cited : (105)

References (48)
  • 1
    • 0024461313 scopus 로고
    • Binding activities of a repertoire of single immunoglobulin variable domains secreted from Escherichia coli
    • Ward E.S., Güssow D., Griffiths A.D., Jones P.T., Winter G. Binding activities of a repertoire of single immunoglobulin variable domains secreted from Escherichia coli. Nature. 341:1989;544-546.
    • (1989) Nature , vol.341 , pp. 544-546
    • Ward, E.S.1    Güssow, D.2    Griffiths, A.D.3    Jones, P.T.4    Winter, G.5
  • 2
    • 0027953603 scopus 로고
    • "camelising" human antibody fragments: NMR studies on VH domains
    • Davies J., Riechmann L. "Camelising" human antibody fragments: NMR studies on VH domains. FEBS Letters. 339:1994;285-290.
    • (1994) FEBS Letters , vol.339 , pp. 285-290
    • Davies, J.1    Riechmann, L.2
  • 6
    • 0037227517 scopus 로고    scopus 로고
    • Biophysical properties of human antibody variable domains
    • Ewert S., Huber T., Honegger A., Plückthun A. Biophysical properties of human antibody variable domains. J. Mol. Biol. 325:2003;531-553.
    • (2003) J. Mol. Biol. , vol.325 , pp. 531-553
    • Ewert, S.1    Huber, T.2    Honegger, A.3    Plückthun, A.4
  • 8
    • 0030767656 scopus 로고    scopus 로고
    • Selection and identification of single domain antibody fragments from camel heavy-chain antibodies
    • Arbabi Ghahroudi M., Desmyter A., Wyns L., Hamers R., Muyldermans S. Selection and identification of single domain antibody fragments from camel heavy-chain antibodies. FEBS Letters. 414:1997;521-526.
    • (1997) FEBS Letters , vol.414 , pp. 521-526
    • Arbabi Ghahroudi, M.1    Desmyter, A.2    Wyns, L.3    Hamers, R.4    Muyldermans, S.5
  • 10
    • 0028168145 scopus 로고
    • Sequence and structure of VH domain from naturally occurring camel heavy chain immunoglobulins lacking light chains
    • Muyldermans S., Atarhouch T., Saldanha J., Barbosa J.A.R.G., Hamers R. Sequence and structure of VH domain from naturally occurring camel heavy chain immunoglobulins lacking light chains. Protein Eng. 7:1994;1129-1135.
    • (1994) Protein Eng. , vol.7 , pp. 1129-1135
    • Muyldermans, S.1    Atarhouch, T.2    Saldanha, J.3    Barbosa, J.A.R.G.4    Hamers, R.5
  • 12
    • 0029746203 scopus 로고    scopus 로고
    • Single antibody domains as small recognition units: Design and in vitro antigen selection of camelized, human VH domains with improved stability
    • Davies J., Riechmann L. Single antibody domains as small recognition units: design and in vitro antigen selection of camelized, human VH domains with improved stability. Protein Eng. 9:1996;531-537.
    • (1996) Protein Eng. , vol.9 , pp. 531-537
    • Davies, J.1    Riechmann, L.2
  • 13
    • 0030922759 scopus 로고    scopus 로고
    • Affinity selection of a camelized V(H) domain antibody inhibitor of hepatitis C virus NS3 protease
    • Martin F., Volpari C., Steinkuhler C., Dimasi N., Brunetti M., Biasiol G., et al. Affinity selection of a camelized V(H) domain antibody inhibitor of hepatitis C virus NS3 protease. Protein Eng. 10:1997;607-614.
    • (1997) Protein Eng. , vol.10 , pp. 607-614
    • Martin, F.1    Volpari, C.2    Steinkuhler, C.3    Dimasi, N.4    Brunetti, M.5    Biasiol, G.6
  • 15
    • 0032763794 scopus 로고    scopus 로고
    • An antibody single-domain phage display library of a native heavy chain variable region: Isolation of functional single-domain VH molecules with a unique interface
    • Reiter Y., Schuck P., Boyd L.F., Plaksin D. An antibody single-domain phage display library of a native heavy chain variable region: isolation of functional single-domain VH molecules with a unique interface. J. Mol. Biol. 290:1999;685-698.
    • (1999) J. Mol. Biol. , vol.290 , pp. 685-698
    • Reiter, Y.1    Schuck, P.2    Boyd, L.F.3    Plaksin, D.4
  • 16
    • 0036570726 scopus 로고    scopus 로고
    • Selection by phage display of llama conventional V(H) fragments with heavy chain antibody V(H)H properties
    • Tanha J., Dubuc G., Hirama T., Narang S.A., MacKenzie C.R. Selection by phage display of llama conventional V(H) fragments with heavy chain antibody V(H)H properties. J. Immunol. Methods. 263:2002;97-109.
    • (2002) J. Immunol. Methods , vol.263 , pp. 97-109
    • Tanha, J.1    Dubuc, G.2    Hirama, T.3    Narang, S.A.4    MacKenzie, C.R.5
  • 25
    • 0032955291 scopus 로고    scopus 로고
    • Comparison of physical chemical properties of llama V(HH) antibody fragments and mouse monoclonal antibodies
    • van der Linden R.H., Frenken L.G., de Geus B., Harmsen M.M., Ruuls R.C., Stok W., et al. Comparison of physical chemical properties of llama V(HH) antibody fragments and mouse monoclonal antibodies. Biochim. Biophys. Acta. 1431:1999;37-46.
    • (1999) Biochim. Biophys. Acta , vol.1431 , pp. 37-46
    • Van Der Linden, R.H.1    Frenken, L.G.2    De Geus, B.3    Harmsen, M.M.4    Ruuls, R.C.5    Stok, W.6
  • 26
    • 0037047012 scopus 로고    scopus 로고
    • Solution structure of a llama single-domain antibody with hydrophobic residues typical of the VH/VL interface
    • Vranken W., Tolkatchev D., Xu P., Tanha J., Chen Z., Narang S., Ni F. Solution structure of a llama single-domain antibody with hydrophobic residues typical of the VH/VL interface. Biochemistry. 41:2002;8570-8579.
    • (2002) Biochemistry , vol.41 , pp. 8570-8579
    • Vranken, W.1    Tolkatchev, D.2    Xu, P.3    Tanha, J.4    Chen, Z.5    Narang, S.6    Ni, F.7
  • 27
    • 0029557830 scopus 로고
    • Thermal stabilization of a single-chain Fv antibody fragment by introduction of a disulphide bond
    • Young N.M., MacKenzie C.R., Narang S.A., Oomen R.P., Baenziger J.E. Thermal stabilization of a single-chain Fv antibody fragment by introduction of a disulphide bond. FEBS Letters. 377:1995;135-139.
    • (1995) FEBS Letters , vol.377 , pp. 135-139
    • Young, N.M.1    MacKenzie, C.R.2    Narang, S.A.3    Oomen, R.P.4    Baenziger, J.E.5
  • 28
    • 0032718607 scopus 로고    scopus 로고
    • Intrabody construction and expression III: Engineering hyperstable V(H) domains
    • Wirtz P., Steipe B. Intrabody construction and expression III: engineering hyperstable V(H) domains. Protein Sci. 8:1999;2245-2250.
    • (1999) Protein Sci. , vol.8 , pp. 2245-2250
    • Wirtz, P.1    Steipe, B.2
  • 29
    • 0040964401 scopus 로고    scopus 로고
    • Different equilibrium stability behaviour of ScFv fragments: Identification, classification, and improvement by protein engineering
    • Wörn A., Plückthun A. Different equilibrium stability behaviour of ScFv fragments: identification, classification, and improvement by protein engineering. Biochemistry. 38:1999;8739-8750.
    • (1999) Biochemistry , vol.38 , pp. 8739-8750
    • Wörn, A.1    Plückthun, A.2
  • 30
    • 0034076282 scopus 로고    scopus 로고
    • The thermal stability of immunoglobulin: Unfolding and aggregation of a multi-domain protein
    • Vermeer A.W.P., Norde W. The thermal stability of immunoglobulin: unfolding and aggregation of a multi-domain protein. Biophys. J. 78:2000;394-404.
    • (2000) Biophys. J. , vol.78 , pp. 394-404
    • Vermeer, A.W.P.1    Norde, W.2
  • 31
    • 0021964141 scopus 로고
    • Measurements of the true affinity constant in solution of antigen-antibody complexes by enzyme-linked immunosorbent assay
    • Friguet B., Chaffotte A.F., Djavadi-Ohaniance L., Goldberg M.E. Measurements of the true affinity constant in solution of antigen-antibody complexes by enzyme-linked immunosorbent assay. J. Immunol. Methods. 77:1985;305-319.
    • (1985) J. Immunol. Methods , vol.77 , pp. 305-319
    • Friguet, B.1    Chaffotte, A.F.2    Djavadi-Ohaniance, L.3    Goldberg, M.E.4
  • 33
    • 0016236512 scopus 로고
    • Crystal and molecular structure of a dimer composed of the variable portions of the Bence-Jones protein REI
    • Epp O., Colman P., Fehlhammer H., Bode W., Schiffer M., Huber R., Palm W. Crystal and molecular structure of a dimer composed of the variable portions of the Bence-Jones protein REI. Eur. J. Biochem. 45:1974;513-524.
    • (1974) Eur. J. Biochem. , vol.45 , pp. 513-524
    • Epp, O.1    Colman, P.2    Fehlhammer, H.3    Bode, W.4    Schiffer, M.5    Huber, R.6    Palm, W.7
  • 35
    • 0031558798 scopus 로고    scopus 로고
    • Standard conformations for the canonical structures of immunoglobulins
    • Al-Lazikani B., Lesk A.M., Chothia C. Standard conformations for the canonical structures of immunoglobulins. J. Mol. Biol. 273:1997;927-948.
    • (1997) J. Mol. Biol. , vol.273 , pp. 927-948
    • Al-Lazikani, B.1    Lesk, A.M.2    Chothia, C.3
  • 36
    • 0035854724 scopus 로고    scopus 로고
    • Antigen specificity and high affinity binding provided by one single loop of a camel single-domain antibody
    • Desmyter A., Decanniere K., Muyldermans S., Wyns L. Antigen specificity and high affinity binding provided by one single loop of a camel single-domain antibody. J. Biol. Chem. 276:2001;26285-26290.
    • (2001) J. Biol. Chem. , vol.276 , pp. 26285-26290
    • Desmyter, A.1    Decanniere, K.2    Muyldermans, S.3    Wyns, L.4
  • 39
    • 0022422660 scopus 로고
    • Nomenclature for incompletely specified bases in nucleic acid sequences: Recommendations 1984
    • Cornish-Bowden A. Nomenclature for incompletely specified bases in nucleic acid sequences: recommendations 1984. Nucl. Acids Res. 13:1985;3021-3030.
    • (1985) Nucl. Acids Res. , vol.13 , pp. 3021-3030
    • Cornish-Bowden, A.1
  • 40
    • 0027955736 scopus 로고
    • X-ray structures of fragments from binding and nonbinding versions of a humanized anti-CD18 antibody: Structural indications of the key role of VH residues 59 to 65
    • Eigenbrot C., Gonzalez T., Mayeda J., Carter P., Werther W., Hotaling T., et al. X-ray structures of fragments from binding and nonbinding versions of a humanized anti-CD18 antibody: structural indications of the key role of VH residues 59 to 65. Proteins: Struct. Funct. Genet. 18:1994;49-62.
    • (1994) Proteins: Struct. Funct. Genet. , vol.18 , pp. 49-62
    • Eigenbrot, C.1    Gonzalez, T.2    Mayeda, J.3    Carter, P.4    Werther, W.5    Hotaling, T.6
  • 41
    • 0000625192 scopus 로고
    • Collaborative Computational Project 4
    • Collaborative Computational Project Number 4. Collaborative Computational Project 4. Acta. Crystallog. sect. D. 1994;760-763.
    • (1994) Acta. Crystallog. Sect. D , pp. 760-763
  • 42
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by linear extrapolation method. 1. Unfolding of phenylmethane-sulfonyl alpha-chymotrypsin using different denaturants
    • Santoro M.M., Bolen D.W. Unfolding free energy changes determined by linear extrapolation method. 1. Unfolding of phenylmethane-sulfonyl alpha-chymotrypsin using different denaturants. Biochemistry. 27:1988;8063-8068.
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2
  • 43
    • 0025420076 scopus 로고
    • Measuring and increasing protein stability
    • Pace C.N. Measuring and increasing protein stability. Trends Biotechnol. 8:1990;93-98.
    • (1990) Trends Biotechnol. , vol.8 , pp. 93-98
    • Pace, C.N.1
  • 44
    • 0002846347 scopus 로고    scopus 로고
    • Measuring the conformational stability of a protein
    • T.E. Creighton. New York: Oxford University Press
    • Pace C.N., Scholtz J.M. Measuring the conformational stability of a protein. Creighton T.E. Protein Structure, A practical Approach. 1997;299-321 Oxford University Press, New York.
    • (1997) Protein Structure, a Practical Approach , pp. 299-321
    • Pace, C.N.1    Scholtz, J.M.2
  • 45
    • 0028820703 scopus 로고
    • Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding
    • Myers J.K., Pace C.N., Scholtz J.M. Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding. Protein Sci. 4:1995;2138-2148.
    • (1995) Protein Sci. , vol.4 , pp. 2138-2148
    • Myers, J.K.1    Pace, C.N.2    Scholtz, J.M.3
  • 46
    • 0024556150 scopus 로고
    • Engineering hybrid genes without the use of restriction enzymes: Gene splicing by overlap extension
    • Horton R.M., Hunt H.D., Ho S.N., Pullen J.K., Pease L.R. Engineering hybrid genes without the use of restriction enzymes: gene splicing by overlap extension. Gene. 77:1989;61-68.
    • (1989) Gene , vol.77 , pp. 61-68
    • Horton, R.M.1    Hunt, H.D.2    Ho, S.N.3    Pullen, J.K.4    Pease, L.R.5
  • 47
    • 0000746745 scopus 로고    scopus 로고
    • Multivariate characterization of molecules for QSAR analysis
    • Goodford P.J. Multivariate characterization of molecules for QSAR analysis. J. Chemom. 10:1996;107-117.
    • (1996) J. Chemom. , vol.10 , pp. 107-117
    • Goodford, P.J.1
  • 48
    • 0033000498 scopus 로고    scopus 로고
    • A structural explanation for the binding of multiple ligands by the alpha-adaptin appendage domain
    • Owen D.J., Vallis Y., Noble M.E., Hunter J.B., Dafforn T.R., Evans P.R., McMahon H.T. A structural explanation for the binding of multiple ligands by the alpha-adaptin appendage domain. Cell. 97:1999;805-815.
    • (1999) Cell , vol.97 , pp. 805-815
    • Owen, D.J.1    Vallis, Y.2    Noble, M.E.3    Hunter, J.B.4    Dafforn, T.R.5    Evans, P.R.6    McMahon, H.T.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.