메뉴 건너뛰기




Volumn 24, Issue 3, 2015, Pages 328-340

Structural features of interfacial tyrosine residue in ROBO1 fibronectin domain-antibody complex: Crystallographic, thermodynamic, and molecular dynamic analyses

Author keywords

antibody engineering; antigen antibody interaction; crystallography; molecular dynamics; thermodynamics

Indexed keywords

IMMUNOGLOBULIN F(AB) FRAGMENT; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY B2212A; ROUNDABOUT GUIDANCE RECEPTOR 1; ROUNDABOUT RECEPTOR; TYROSINE; UNCLASSIFIED DRUG; FIBRONECTIN; IMMUNOGLOBULIN RECEPTOR; NERVE PROTEIN; RECOMBINANT PROTEIN;

EID: 84957108848     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.2619     Document Type: Article
Times cited : (18)

References (40)
  • 1
    • 0035524114 scopus 로고    scopus 로고
    • Improving the efficacy of antibody-based cancer therapies
    • Carter P, (2001) Improving the efficacy of antibody-based cancer therapies. Nat Rev Cancer 1: 118-129.
    • (2001) Nat Rev Cancer , vol.1 , pp. 118-129
    • Carter, P.1
  • 2
    • 11244265898 scopus 로고    scopus 로고
    • Identification and validation of cell surface antigens for antibody targeting in oncology
    • Carter P, Smith L, Ryan M, (2004) Identification and validation of cell surface antigens for antibody targeting in oncology. Endocr Relat Cancer 11: 659-687.
    • (2004) Endocr Relat Cancer , vol.11 , pp. 659-687
    • Carter, P.1    Smith, L.2    Ryan, M.3
  • 5
    • 35148855712 scopus 로고    scopus 로고
    • Computational design of antibody-affinity improvement beyond in vivo maturation
    • Lippow SM, Wittrup KD, Tidor B, (2007) Computational design of antibody-affinity improvement beyond in vivo maturation. Nat Biotechnol 25: 1171-1176.
    • (2007) Nat Biotechnol , vol.25 , pp. 1171-1176
    • Lippow, S.M.1    Wittrup, K.D.2    Tidor, B.3
  • 6
    • 0025964038 scopus 로고
    • Structure, function and properties of antibody binding sites
    • Mian IS, Bradwell AR, Olson AJ, (1991) Structure, function and properties of antibody binding sites. J Mol Biol 217: 133-151.
    • (1991) J Mol Biol , vol.217 , pp. 133-151
    • Mian, I.S.1    Bradwell, A.R.2    Olson, A.J.3
  • 7
    • 4344714933 scopus 로고    scopus 로고
    • Synthetic antibodies from a four-amino-acid code: A dominant role for tyrosine in antigen recognition
    • Fellouse FA, Wiesmann C, Sidhu SS, (2004) Synthetic antibodies from a four-amino-acid code: a dominant role for tyrosine in antigen recognition. Proc Natl Acad Sci USA 101: 12467-12472.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 12467-12472
    • Fellouse, F.A.1    Wiesmann, C.2    Sidhu, S.S.3
  • 8
    • 34250315356 scopus 로고    scopus 로고
    • Structural consequences of mutations in interfacial Tyr residues of a protein antigen-antibody complex. The case of HyHEL-10-HEL
    • Shiroishi M, Tsumoto K, Tanaka Y, Yokota A, Nakanishi T, Kondo H, Kumagai I, (2007) Structural consequences of mutations in interfacial Tyr residues of a protein antigen-antibody complex. The case of HyHEL-10-HEL. J Biol Chem 282: 6783-6791.
    • (2007) J Biol Chem , vol.282 , pp. 6783-6791
    • Shiroishi, M.1    Tsumoto, K.2    Tanaka, Y.3    Yokota, A.4    Nakanishi, T.5    Kondo, H.6    Kumagai, I.7
  • 9
    • 65749099472 scopus 로고    scopus 로고
    • The importance of being tyrosine: Lessons in molecular recognition from minimalist synthetic binding proteins
    • Koide S, Sidhu SS, (2009) The importance of being tyrosine: lessons in molecular recognition from minimalist synthetic binding proteins. ACS Chem Biol 4: 325-334.
    • (2009) ACS Chem Biol , vol.4 , pp. 325-334
    • Koide, S.1    Sidhu, S.S.2
  • 10
    • 0033056238 scopus 로고    scopus 로고
    • Improving antibody affinity by mimicking somatic hypermutation in vitro
    • Chowdhury PS, Pastan I, (1999) Improving antibody affinity by mimicking somatic hypermutation in vitro. Nat Biotechnol 17: 568-572.
    • (1999) Nat Biotechnol , vol.17 , pp. 568-572
    • Chowdhury, P.S.1    Pastan, I.2
  • 13
    • 0032559219 scopus 로고    scopus 로고
    • Roundabout controls axon crossing of the CNS midline and defines a novel subfamily of evolutionarily conserved guidance receptors
    • Kidd T, Brose K, Mitchell KJ, Fetter RD, Tessier-Lavigne M, Goodman CS, Tear G, (1998) Roundabout controls axon crossing of the CNS midline and defines a novel subfamily of evolutionarily conserved guidance receptors. Cell 92: 205-215.
    • (1998) Cell , vol.92 , pp. 205-215
    • Kidd, T.1    Brose, K.2    Mitchell, K.J.3    Fetter, R.D.4    Tessier-Lavigne, M.5    Goodman, C.S.6    Tear, G.7
  • 18
    • 33646191863 scopus 로고    scopus 로고
    • Ig-like domains on bacteriophages: A tale of promiscuity and deceit
    • Fraser JS, Yu Z, Maxwell KL, Davidson AR, (2006) Ig-like domains on bacteriophages: a tale of promiscuity and deceit. J Mol Biol 359: 496-507.
    • (2006) J Mol Biol , vol.359 , pp. 496-507
    • Fraser, J.S.1    Yu, Z.2    Maxwell, K.L.3    Davidson, A.R.4
  • 19
    • 70349314669 scopus 로고    scopus 로고
    • FN3: A new protein scaffold reaches the clinic
    • Bloom L, Calabro V, (2009) FN3: a new protein scaffold reaches the clinic. Drug Discov Today 14: 949-955.
    • (2009) Drug Discov Today , vol.14 , pp. 949-955
    • Bloom, L.1    Calabro, V.2
  • 21
    • 0030040277 scopus 로고    scopus 로고
    • Interactions of protein antigens with antibodies
    • Davies DR, Cohen GH, (1996) Interactions of protein antigens with antibodies. Proc Natl Acad Sci USA 93: 7-12.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 7-12
    • Davies, D.R.1    Cohen, G.H.2
  • 22
    • 0036420965 scopus 로고    scopus 로고
    • Molecular recognition in antibody-antigen complexes
    • Janin J. Wodak S.J. Eds., Vol. Amsterdam: Elsevier
    • Sundberg EJ, Mariuzza RA, Molecular recognition in antibody-antigen complexes. In:, Janin J, Wodak SJ, Eds. (2002) Advanced in Protein Chemistry, Vol 61. Amsterdam: Elsevier, pp 119-160.
    • (2002) Advanced in Protein Chemistry , vol.61 , pp. 119-160
    • Sundberg, E.J.1    Mariuzza, R.A.2
  • 23
    • 0027772959 scopus 로고
    • Shape complementarity at protein/protein interfaces
    • Lawrence MC, Colman PM, (1993) Shape complementarity at protein/protein interfaces. J Mol Biol 234: 946-950.
    • (1993) J Mol Biol , vol.234 , pp. 946-950
    • Lawrence, M.C.1    Colman, P.M.2
  • 24
    • 0036469060 scopus 로고    scopus 로고
    • Unraveling hot spots in binding interfaces: Progress and challenges
    • DeLano WL, (2002) Unraveling hot spots in binding interfaces: progress and challenges. Curr Opin Struct Biol 12: 14-20.
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 14-20
    • DeLano, W.L.1
  • 25
    • 0003187567 scopus 로고    scopus 로고
    • The atomic structure of protein-protein recognition sites
    • Lo Conte L, Chothia C, Janin J, (1999) The atomic structure of protein-protein recognition sites. J Mol Biol 285: 2177-2198.
    • (1999) J Mol Biol , vol.285 , pp. 2177-2198
    • Lo Conte, L.1    Chothia, C.2    Janin, J.3
  • 26
    • 33644783935 scopus 로고    scopus 로고
    • Tyrosine plays a dominant functional role in the paratope of a synthetic antibody derived from a four amino acid code
    • Fellouse FA, Barthelemy PA, Kelley RF, Sidhu SS, (2006) Tyrosine plays a dominant functional role in the paratope of a synthetic antibody derived from a four amino acid code. J Mol Biol 357: 100-114.
    • (2006) J Mol Biol , vol.357 , pp. 100-114
    • Fellouse, F.A.1    Barthelemy, P.A.2    Kelley, R.F.3    Sidhu, S.S.4
  • 27
    • 84863246128 scopus 로고    scopus 로고
    • Antigen-binding site anatomy and somatic mutations in antibodies that recognize different types of antigens
    • Raghunathan G, Smart J, Williams J, Almagro JC, (2012) Antigen-binding site anatomy and somatic mutations in antibodies that recognize different types of antigens. J Mol Recognit 25: 103-113.
    • (2012) J Mol Recognit , vol.25 , pp. 103-113
    • Raghunathan, G.1    Smart, J.2    Williams, J.3    Almagro, J.C.4
  • 28
    • 52049123291 scopus 로고    scopus 로고
    • Do enthalpy and entropy distinguish first in class from best in class?
    • Freire E, (2008) Do enthalpy and entropy distinguish first in class from best in class? Drug Discov Today 13: 869-874.
    • (2008) Drug Discov Today , vol.13 , pp. 869-874
    • Freire, E.1
  • 30
    • 77953725797 scopus 로고    scopus 로고
    • Human ROBO1 is cleaved by metalloproteinases and gamma-secretase and migrates to the nucleus in cancer cells
    • Seki M, Watanabe A, Enomoto S, Kawamura T, Ito H, Kodama T, Hamakubo T, Aburatani H, (2010) Human ROBO1 is cleaved by metalloproteinases and gamma-secretase and migrates to the nucleus in cancer cells. FEBS Lett 584: 2909-2915.
    • (2010) FEBS Lett , vol.584 , pp. 2909-2915
    • Seki, M.1    Watanabe, A.2    Enomoto, S.3    Kawamura, T.4    Ito, H.5    Kodama, T.6    Hamakubo, T.7    Aburatani, H.8
  • 31
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Ötwinowski Z, Minor W, (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276: 307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Ötwinowski, Z.1    Minor, W.2
  • 37
  • 38
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel E, Henrick K, (2007) Inference of macromolecular assemblies from crystalline state. J Mol Biol 372: 774-797.
    • (2007) J Mol Biol , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 39
    • 65249106601 scopus 로고    scopus 로고
    • High-level ab initio calculations to Improve protein backbone dihedral parameters
    • Fujitani H, Matsuura A, Sakai S, Sato H, Tanida Y, (2009) High-level ab initio calculations to Improve protein backbone dihedral parameters. J Chem Theory Comput 5: 1155-1165.
    • (2009) J Chem Theory Comput , vol.5 , pp. 1155-1165
    • Fujitani, H.1    Matsuura, A.2    Sakai, S.3    Sato, H.4    Tanida, Y.5
  • 40
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • Hess B, Kutzner C, Van Der Spoel D, Lindahl E, (2008) GROMACS 4: algorithms for highly efficient, load-balanced, and scalable molecular simulation. J Chem Theory Comput 4: 435-447.
    • (2008) J Chem Theory Comput , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3    Lindahl, E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.