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Volumn 13, Issue 1, 2013, Pages

Crystal structure of signal regulatory protein gamma (SIRPγ) in complex with an antibody Fab fragment

Author keywords

Antigen binding complex; Receptor structure; Signal regulatory protein

Indexed keywords

IMMUNOGLOBULIN F(AB) FRAGMENT; INTEGRIN; MONOMER; REGULATOR PROTEIN; SIGNAL REGULATORY PROTEIN GAMMA; UNCLASSIFIED DRUG; ANTIGEN ANTIBODY COMPLEX; CELL SURFACE RECEPTOR; DIFFERENTIATION ANTIGEN; IMMUNOGLOBULIN RECEPTOR; RECOMBINANT PROTEIN; SIRPA PROTEIN, HUMAN; SIRPB1 PROTEIN, HUMAN; SIRPG PROTEIN, HUMAN;

EID: 84879814551     PISSN: None     EISSN: 14726807     Source Type: Journal    
DOI: 10.1186/1472-6807-13-13     Document Type: Article
Times cited : (11)

References (32)
  • 1
    • 33745712879 scopus 로고    scopus 로고
    • The SIRP family of receptors and immune regulation
    • 10.1038/nri1859 16691243
    • The SIRP family of receptors and immune regulation. Barclay AN, Brown MH, Nat Rev Immunol 2006 6 6 457 464 10.1038/nri1859 16691243
    • (2006) Nat Rev Immunol , vol.6 , Issue.6 , pp. 457-464
    • Barclay, A.N.1    Brown, M.H.2
  • 2
    • 64049091276 scopus 로고    scopus 로고
    • Signal regulatory protein alpha (SIRPalpha)/CD47 interaction and function
    • Epub 2009 Feb 2014 10.1016/j.coi.2009.01.008 19223164
    • Signal regulatory protein alpha (SIRPalpha)/CD47 interaction and function. Barclay AN, Curr Opin Immunol 2009 21 1 47 52 Epub 2009 Feb 2014 10.1016/j.coi.2009.01.008 19223164
    • (2009) Curr Opin Immunol , vol.21 , Issue.1 , pp. 47-52
    • Barclay, A.N.1
  • 3
    • 4043068511 scopus 로고    scopus 로고
    • Human lymphocytes interact directly with CD47 through a novel member of the signal regulatory protein (SIRP) family
    • Human lymphocytes interact directly with CD47 through a novel member of the signal regulatory protein (SIRP) family. Brooke G, Holbrook JD, Brown MH, Barclay AN, J Immunol 2004 173 4 2562 2570 15294972 (Pubitemid 39063115)
    • (2004) Journal of Immunology , vol.173 , Issue.4 , pp. 2562-2570
    • Brooke, G.1    Holbrook, J.D.2    Brown, M.H.3    Barclay, A.N.4
  • 4
    • 15244347763 scopus 로고    scopus 로고
    • Adhesion of human T cells to antigen-presenting cells through SIRPβ2-CD47 interaction costimulates T-cell proliferation
    • DOI 10.1182/blood-2004-07-2823
    • Adhesion of human T cells to antigen-presenting cells through SIRPbeta2-CD47 interaction costimulates T-cell proliferation. Piccio L, Vermi W, Boles KS, Fuchs A, Strader CA, Facchetti F, Cella M, Colonna M, Blood 2005 105 6 2421 2427 10.1182/blood-2004-07-2823 15383453 (Pubitemid 40387041)
    • (2005) Blood , vol.105 , Issue.6 , pp. 2421-2427
    • Piccio, L.1    Vermi, W.2    Boles, K.S.3    Fuchs, A.4    Strader, C.A.5    Facchetti, F.6    Cella, M.7    Colonna, M.8
  • 8
    • 0346961787 scopus 로고    scopus 로고
    • On the origins of adaptive immunity: Innate immune receptors join the tale
    • DOI 10.1016/j.it.2003.11.006
    • On the origins of adaptive immunity: innate immune receptors join the tale. Van den Berg TK, Yoder JA, Litman GW, Trends Immunol 2004 25 1 11 16 10.1016/j.it.2003.11.006 14698279 (Pubitemid 38032803)
    • (2004) Trends in Immunology , vol.25 , Issue.1 , pp. 11-16
    • Van Den Berg, T.K.1    Yoder, J.A.2    Litman, G.W.3
  • 9
    • 34347235840 scopus 로고    scopus 로고
    • The structure of the macrophage signal regulatory protein α (SIRPα) inhibitory receptor reveals a binding face reminiscent of that used by T cell receptors
    • DOI 10.1074/jbc.M611511200
    • The structure of the macrophage signal regulatory protein alpha (SIRPalpha) inhibitory receptor reveals a binding face reminiscent of that used by T cell receptors. Hatherley D, Harlos K, Dunlop DC, Stuart DI, Barclay AN, J Biol Chem 2007 282 19 14567 14575 10.1074/jbc.M611511200 17369261 (Pubitemid 47100437)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.19 , pp. 14567-14575
    • Hatherley, D.1    Harlos, K.2    Dunlop, D.C.3    Stuart, D.I.4    Barclay, A.N.5
  • 11
    • 47349105855 scopus 로고    scopus 로고
    • Paired Receptor Specificity Explained by Structures of Signal Regulatory Proteins Alone and Complexed with CD47
    • DOI 10.1016/j.molcel.2008.05.026, PII S1097276508004346
    • Paired receptor specificity explained by structures of signal regulatory proteins alone and complexed with CD47. Hatherley D, Graham SC, Turner J, Harlos K, Stuart DI, Barclay AN, Mol Cell 2008 31 2 266 277 10.1016/j.molcel.2008.05. 026 18657508 (Pubitemid 352001399)
    • (2008) Molecular Cell , vol.31 , Issue.2 , pp. 266-277
    • Hatherley, D.1    Graham, S.C.2    Turner, J.3    Harlos, K.4    Stuart, D.I.5    Barclay, A.N.6
  • 12
    • 70350353206 scopus 로고    scopus 로고
    • Structure of signal-regulatory protein alpha: A link to antigen receptor evolution
    • 10.1074/jbc.M109.017566 19628875
    • Structure of signal-regulatory protein alpha: a link to antigen receptor evolution. Hatherley D, Graham SC, Harlos K, Stuart DI, Barclay AN, J Biol Chem 2009 284 39 26613 26619 10.1074/jbc.M109.017566 19628875
    • (2009) J Biol Chem , vol.284 , Issue.39 , pp. 26613-26619
    • Hatherley, D.1    Graham, S.C.2    Harlos, K.3    Stuart, D.I.4    Barclay, A.N.5
  • 13
    • 0029646090 scopus 로고
    • The use of antibody fragments for crystallization and structure determinations
    • DOI 10.1016/S0969-2126(01)00266-0
    • The use of antibody fragments for crystallization and structure determinations. Kovari LC, Momany C, Rossmann MG, Structure 1995 3 12 1291 1293 10.1016/S0969-2126(01)00266-0 8747455 (Pubitemid 3012182)
    • (1995) Structure , vol.3 , Issue.12 , pp. 1291-1293
    • Kovari, L.C.1    Momany, C.2    Rossmann, M.G.3
  • 14
    • 61349101955 scopus 로고    scopus 로고
    • Overview on concepts and applications of Fab antibody fragments
    • Overview on concepts and applications of Fab antibody fragments. Rader C, Curr Protoc Protein Sci 2009 6 6 6 9
    • (2009) Curr Protoc Protein Sci , vol.6 , Issue.6 , pp. 6-9
    • Rader, C.1
  • 15
    • 52949116784 scopus 로고    scopus 로고
    • A pipeline for the production of antibody fragments for structural studies using transient expression in HEK 293T cells
    • 10.1016/j.pep.2008.06.017 18662785
    • A pipeline for the production of antibody fragments for structural studies using transient expression in HEK 293T cells. Nettleship JE, Ren J, Rahman N, Berrow NS, Hatherley D, Barclay AN, Owens RJ, Protein Expr Purif 2008 62 1 83 89 10.1016/j.pep.2008.06.017 18662785
    • (2008) Protein Expr Purif , vol.62 , Issue.1 , pp. 83-89
    • Nettleship, J.E.1    Ren, J.2    Rahman, N.3    Berrow, N.S.4    Hatherley, D.5    Barclay, A.N.6    Owens, R.J.7
  • 16
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • DOI 10.1107/S0907444904026460
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Krissinel E, Henrick K, Acta Crystallogr D: Biol Crystallogr 2004 60 Pt 12 Pt 1 2256 2268 (Pubitemid 41742778)
    • (2004) Acta Crystallographica Section D: Biological Crystallography , vol.60 , Issue.12 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 17
    • 34147167680 scopus 로고    scopus 로고
    • On the relationship between sequence and structure similarities in proteomics
    • DOI 10.1093/bioinformatics/btm006
    • On the relationship between sequence and structure similarities in proteomics. Krissinel E, Bioinformatics 2007 23 6 717 723 10.1093/ bioinformatics/btm006 17242029 (Pubitemid 46554723)
    • (2007) Bioinformatics , vol.23 , Issue.6 , pp. 717-723
    • Krissinel, E.1
  • 18
    • 0003187567 scopus 로고    scopus 로고
    • The atomic structure of protein-protein recognition sites
    • DOI 10.1006/jmbi.1998.2439
    • The atomic structure of protein-protein recognition sites. Lo Conte L, Chothia C, Janin J, J Mol Biol 1999 285 5 2177 2198 10.1006/jmbi.1998.2439 9925793 (Pubitemid 29078179)
    • (1999) Journal of Molecular Biology , vol.285 , Issue.5 , pp. 2177-2198
    • Conte, L.L.1    Chothia, C.2    Janin, J.3
  • 19
    • 77950552976 scopus 로고    scopus 로고
    • The implementation of SOMO (SOlution MOdeller) in the UltraScan analytical ultracentrifugation data analysis suite: Enhanced capabilities allow the reliable hydrodynamic modeling of virtually any kind of biomacromolecule
    • 10.1007/s00249-009-0418-0 19234696
    • The implementation of SOMO (SOlution MOdeller) in the UltraScan analytical ultracentrifugation data analysis suite: enhanced capabilities allow the reliable hydrodynamic modeling of virtually any kind of biomacromolecule. Brookes E, Demeler B, Rosano C, Rocco M, Eur Biophys J 2010 39 423 435 10.1007/s00249-009-0418-0 19234696
    • (2010) Eur Biophys J , vol.39 , pp. 423-435
    • Brookes, E.1    Demeler, B.2    Rosano, C.3    Rocco, M.4
  • 22
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling. Schuck P, Biophys J 2000 78 1606 1619 10.1016/S0006-3495(00)76713-0 10692345 (Pubitemid 30141584)
    • (2000) Biophysical Journal , vol.78 , Issue.3 , pp. 1606-1619
    • Schuck, P.1
  • 23
    • 1442274756 scopus 로고    scopus 로고
    • Sedimentation equilibrium analysis of protein interactions with global implicit mass conservation constraints and systematic noise decomposition
    • DOI 10.1016/j.ab.2003.12.014, PII S0003269704000363
    • Sedimentation equilibrium analysis of protein interactions with global implicit mass conservation constraints and systematic noise decomposition. Vistica J, Dam J, Balbo A, Yikilmaz E, Mariuzza RA, Rouault TA, Schuck P, Anal Biochem 2004 326 234 256 10.1016/j.ab.2003.12.014 15003564 (Pubitemid 38293385)
    • (2004) Analytical Biochemistry , vol.326 , Issue.2 , pp. 234-256
    • Vistica, J.1    Dam, J.2    Balbo, A.3    Yikilmaz, E.4    Mariuzza, R.A.5    Rouault, T.A.6    Schuck, P.7
  • 25
    • 0021729671 scopus 로고
    • Glycosylation mutants of animal cells
    • 10.1146/annurev.ge.18.120184.002521 6241454
    • Glycosylation mutants of animal cells. Stanley P, Annu Rev Genet 1984 18 525 552 10.1146/annurev.ge.18.120184.002521 6241454
    • (1984) Annu Rev Genet , vol.18 , pp. 525-552
    • Stanley, P.1
  • 26
    • 84934443100 scopus 로고    scopus 로고
    • The production of glycoproteins by transient expression in mammalian cells
    • 10.1007/978-1-59745-196-3-16 18988030
    • The production of glycoproteins by transient expression in mammalian cells. Nettleship JE, Rahman-Huq N, Owens RJ, Methods Mol Biol 2009 498 245 263 10.1007/978-1-59745-196-3-16 18988030
    • (2009) Methods Mol Biol , vol.498 , pp. 245-263
    • Nettleship, J.E.1    Rahman-Huq, N.2    Owens, R.J.3
  • 27
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Processing of X-ray diffraction data collected in oscillation mode. Otwinowski ZMW, Methods Enzymol 1997 276 307 326
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.M.W.1
  • 28
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An Automated Program for Molecular Replacement
    • MOLREP: an automated program for molecular replacement. Vagin A A, Teplyakov A, J Appl Cryst 1997 30 1022 1025 10.1107/S0021889897006766 (Pubitemid 127485985)
    • (1997) Journal of Applied Crystallography , vol.30 , Issue.6 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 31
    • 0018792428 scopus 로고
    • Crystal structure of cat muscle pyruvate kinase at a resolution of 2.6 A
    • 10.1016/0022-2836(79)90416-9 537059
    • Crystal structure of cat muscle pyruvate kinase at a resolution of 2.6 A. Stuart DI, Levine M, Muirhead H, Stammers DK, J Mol Biol 1979 134 1 109 142 10.1016/0022-2836(79)90416-9 537059
    • (1979) J Mol Biol , vol.134 , Issue.1 , pp. 109-142
    • Stuart, D.I.1    Levine, M.2    Muirhead, H.3    Stammers, D.K.4


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