메뉴 건너뛰기




Volumn 105, Issue 34, 2008, Pages 12254-12258

Crystal structures of fibronectin-binding sites from Staphylococcus aureus FnBPA in complex with fibronectin domains

Author keywords

Host pathogen interaction; Intrinsic disorder; Tandem zipper

Indexed keywords

FIBRONECTIN;

EID: 50449095346     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0803556105     Document Type: Article
Times cited : (115)

References (34)
  • 1
    • 0032551901 scopus 로고    scopus 로고
    • Staphylococcus aureus infections
    • Lowy FD (1998) Staphylococcus aureus infections. N Engl J Med 339:520-532.
    • (1998) N Engl J Med , vol.339 , pp. 520-532
    • Lowy, F.D.1
  • 3
    • 0023654797 scopus 로고
    • Isolation and characterization of a fibronectin receptor from Staphylococcus-aureus
    • Froman G, Switalski LM, Speziale P, Höök M(1987) Isolation and characterization of a fibronectin receptor from Staphylococcus-aureus. J Biol Chem 262:6564-6571.
    • (1987) J Biol Chem , vol.262 , pp. 6564-6571
    • Froman, G.1    Switalski, L.M.2    Speziale, P.3    Höök, M.4
  • 4
    • 0037653702 scopus 로고    scopus 로고
    • Pathogenic bacteria attach to human fibronectin through a tandem beta-zipper
    • Schwarz-Linek U, et al. (2003) Pathogenic bacteria attach to human fibronectin through a tandem beta-zipper. Nature 423:177-181.
    • (2003) Nature , vol.423 , pp. 177-181
    • Schwarz-Linek, U.1
  • 5
    • 34548494596 scopus 로고    scopus 로고
    • The tandem β-zipper model defines high affinity fibronectin-binding repeats within Staphylococcus aureus FnBPA
    • Meenan NAG, et al. (2007) The tandem β-zipper model defines high affinity fibronectin-binding repeats within Staphylococcus aureus FnBPA. J Biol Chem 282:25893-25902.
    • (2007) J Biol Chem , vol.282 , pp. 25893-25902
    • Meenan, N.A.G.1
  • 6
    • 21144433633 scopus 로고    scopus 로고
    • Fibrinogen and fibronectin binding cooperate for valve infection and invasion in Staphylococcus aureus experimental endocarditis
    • Que Y-A, et al. (2005) Fibrinogen and fibronectin binding cooperate for valve infection and invasion in Staphylococcus aureus experimental endocarditis. J Exp Med 201:1627-1635.
    • (2005) J Exp Med , vol.201 , pp. 1627-1635
    • Que, Y.-A.1
  • 7
    • 0033396514 scopus 로고    scopus 로고
    • Bacterial fibronectin-binding proteins and endothelial cell surface fibronectin mediate adherence of Staphylococcus aureus to resting human endothelial cells
    • Peacock SJ, Foster TJ, Cameron BJ, Berendt AR (1999) Bacterial fibronectin-binding proteins and endothelial cell surface fibronectin mediate adherence of Staphylococcus aureus to resting human endothelial cells. Microbiology 145:3477-3486.
    • (1999) Microbiology , vol.145 , pp. 3477-3486
    • Peacock, S.J.1    Foster, T.J.2    Cameron, B.J.3    Berendt, A.R.4
  • 8
    • 34247128762 scopus 로고    scopus 로고
    • Fibronectin-binding proteins and clumping factor A in Staphylococcus aureus experimental endocarditis: FnBPA is sufficient to activate human endothelial cells
    • Heying R, van de Gevel J, Que Y-A, Moreillon P, Beekhuizen H (2007) Fibronectin-binding proteins and clumping factor A in Staphylococcus aureus experimental endocarditis: FnBPA is sufficient to activate human endothelial cells. Thromb Haemost 97:617-626.
    • (2007) Thromb Haemost , vol.97 , pp. 617-626
    • Heying, R.1    van de Gevel, J.2    Que, Y.-A.3    Moreillon, P.4    Beekhuizen, H.5
  • 9
    • 33646854563 scopus 로고    scopus 로고
    • The interaction of bacterial pathogens with platelets
    • Fitzgerald JR, Foster TJ, Cox D (2006) The interaction of bacterial pathogens with platelets. Nat Rev Micro 4:445-457.
    • (2006) Nat Rev Micro , vol.4 , pp. 445-457
    • Fitzgerald, J.R.1    Foster, T.J.2    Cox, D.3
  • 10
    • 33645760425 scopus 로고    scopus 로고
    • The role of Staphylococcus aureus adhesins in the pathogenesis of ventricular assist device-related infections
    • Arrecubieta C, et al. (2006) The role of Staphylococcus aureus adhesins in the pathogenesis of ventricular assist device-related infections. J Infect Dis 193:1109-1119.
    • (2006) J Infect Dis , vol.193 , pp. 1109-1119
    • Arrecubieta, C.1
  • 11
    • 0003187567 scopus 로고    scopus 로고
    • The atomic structure of protein-protein recognition sites
    • Conte LL, 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
    • Conte, L.L.1    Chothia, C.2    Janin, J.3
  • 12
    • 34547943482 scopus 로고    scopus 로고
    • Molecular principles of the interactions of disordered proteins
    • Meszaros B, Tompa P, Simon I, Dosztanyi Z (2007) Molecular principles of the interactions of disordered proteins. J Mol Biol 372:549-561.
    • (2007) J Mol Biol , vol.372 , pp. 549-561
    • Meszaros, B.1    Tompa, P.2    Simon, I.3    Dosztanyi, Z.4
  • 13
    • 33746300776 scopus 로고    scopus 로고
    • Protein-protein interaction through β-strand addition
    • Remaut H, Waksman G (2006) Protein-protein interaction through β-strand addition. Trends Biochem Sci 31:436.
    • (2006) Trends Biochem Sci , vol.31 , pp. 436
    • Remaut, H.1    Waksman, G.2
  • 14
    • 5044224710 scopus 로고    scopus 로고
    • Tandem LIM domains provide synergistic binding in the LMO4:Ldb1 complex
    • Deane JE, et al. (2004) Tandem LIM domains provide synergistic binding in the LMO4:Ldb1 complex. EMBO J 23:3589-3598.
    • (2004) EMBO J , vol.23 , pp. 3589-3598
    • Deane, J.E.1
  • 15
    • 4644293801 scopus 로고    scopus 로고
    • High affinity streptococcal binding to human fibronectin requires specific recognition of sequential F1 modules
    • Schwarz-Linek U, et al. (2004) High affinity streptococcal binding to human fibronectin requires specific recognition of sequential F1 modules. J Biol Chem 279:39017-39025.
    • (2004) J Biol Chem , vol.279 , pp. 39017-39025
    • Schwarz-Linek, U.1
  • 16
    • 34047133711 scopus 로고    scopus 로고
    • The solution and crystal structures of amodule pair from the Staphylococcus aureus-binding site of human fibronectin - A tale with a twist
    • Rudino-Pinera E, et al. (2007) The solution and crystal structures of amodule pair from the Staphylococcus aureus-binding site of human fibronectin - A tale with a twist. J Mol Biol 368:833-844.
    • (2007) J Mol Biol , vol.368 , pp. 833-844
    • Rudino-Pinera, E.1
  • 17
    • 0026694034 scopus 로고
    • Towards an understanding of the arginine-aspartate interaction
    • Mitchell JBO, Thornton JM, Singh J, Price SL (1992) Towards an understanding of the arginine-aspartate interaction. J Mol Biol 226:251-262.
    • (1992) J Mol Biol , vol.226 , pp. 251-262
    • Mitchell, J.B.O.1    Thornton, J.M.2    Singh, J.3    Price, S.L.4
  • 18
    • 5644266080 scopus 로고    scopus 로고
    • Interaction of Staphylococcus aureus fibronectin-binding protein with fibronectin: Affinity, stoichiometry, and modular requirements
    • Ingham KC, Brew S, Vaz D, Sauder DN, McGavin MJ (2004) Interaction of Staphylococcus aureus fibronectin-binding protein with fibronectin: affinity, stoichiometry, and modular requirements. J Biol Chem 279:42945-42953.
    • (2004) J Biol Chem , vol.279 , pp. 42945-42953
    • Ingham, K.C.1    Brew, S.2    Vaz, D.3    Sauder, D.N.4    McGavin, M.J.5
  • 19
    • 33748209542 scopus 로고    scopus 로고
    • Fibronectin-binding proteins of Gram-positive cocci
    • Schwarz-Linek U, Höök M, Potts JR (2006) Fibronectin-binding proteins of Gram-positive cocci. Microbes Infect 8:2291-2298.
    • (2006) Microbes Infect , vol.8 , pp. 2291-2298
    • Schwarz-Linek, U.1    Höök, M.2    Potts, J.R.3
  • 20
    • 0034883769 scopus 로고    scopus 로고
    • De novo formation of focal complex-like structures in host cells by invading streptococci
    • Ozeri V, et al. (2001) De novo formation of focal complex-like structures in host cells by invading streptococci. Mol Microbiol 41:561-573.
    • (2001) Mol Microbiol , vol.41 , pp. 561-573
    • Ozeri, V.1
  • 21
    • 0032374091 scopus 로고    scopus 로고
    • Structural and dynamical characterization of a biologically active unfolded fibronectin-binding protein from Staphylococcus aureus
    • Penkett CJ, et al. (1998) Structural and dynamical characterization of a biologically active unfolded fibronectin-binding protein from Staphylococcus aureus. Biochemistry 37:17054-17067.
    • (1998) Biochemistry , vol.37 , pp. 17054-17067
    • Penkett, C.J.1
  • 22
    • 0030051158 scopus 로고    scopus 로고
    • Conformational changes in the fibronectin binding MSCRAMMs are induced by ligand binding
    • HousePompeo K, Xu Y, Joh D, Speziale P, Höök M(1996) Conformational changes in the fibronectin binding MSCRAMMs are induced by ligand binding. J Biol Chem 271:1379-1384.
    • (1996) J Biol Chem , vol.271 , pp. 1379-1384
    • HousePompeo, K.1    Xu, Y.2    Joh, D.3    Speziale, P.4    Höök, M.5
  • 23
    • 0035022941 scopus 로고    scopus 로고
    • Intrinsically disordered protein
    • Dunker AK, et al. (2001) Intrinsically disordered protein. J Mol Graphics Model 19:26-59.
    • (2001) J Mol Graphics Model , vol.19 , pp. 26-59
    • Dunker, A.K.1
  • 24
    • 25144472591 scopus 로고    scopus 로고
    • Showing your ID: Intrinsic disorder as an ID for recognition, regulation and cell signaling
    • Uversky VN, Oldfield CJ, Dunker AK (2005) Showing your ID: Intrinsic disorder as an ID for recognition, regulation and cell signaling. J Mol Recognit 18:343-384.
    • (2005) J Mol Recognit , vol.18 , pp. 343-384
    • Uversky, V.N.1    Oldfield, C.J.2    Dunker, A.K.3
  • 25
    • 0037309985 scopus 로고    scopus 로고
    • Extended disordered proteins: Targeting function with less scaffold
    • Gunasekaran K, et al (2003) Extended disordered proteins: targeting function with less scaffold. Trends Biochem Sci 28:81-85.
    • (2003) Trends Biochem Sci , vol.28 , pp. 81-85
    • Gunasekaran, K.1
  • 26
    • 33846099868 scopus 로고    scopus 로고
    • DisProt: The database of disordered proteins
    • Sickmeier M, et al. (2007) DisProt: the database of disordered proteins. Nucleic Acids Res 35:D786-D793.
    • (2007) Nucleic Acids Res , vol.35
    • Sickmeier, M.1
  • 27
    • 34249067404 scopus 로고    scopus 로고
    • Interdomain association in fibronectin: Insight into cryptic sites and fibrillogenesis
    • Vakonakis I, Staunton D, Campbell ID (2007) Interdomain association in fibronectin: insight into cryptic sites and fibrillogenesis. EMBO J 26:2575-2583.
    • (2007) EMBO J , vol.26 , pp. 2575-2583
    • Vakonakis, I.1    Staunton, D.2    Campbell, I.D.3
  • 28
    • 21444441457 scopus 로고    scopus 로고
    • Borrelia burgdorferi binds fibronectin through a tandem beta zipper- a common mechanism of fibronectin binding in staphylococci, streptococci and spirochetes
    • Raibaud S, et al. (2005) Borrelia burgdorferi binds fibronectin through a tandem beta zipper- a common mechanism of fibronectin binding in staphylococci, streptococci and spirochetes. J Biol Chem 280:18803-18809.
    • (2005) J Biol Chem , vol.280 , pp. 18803-18809
    • Raibaud, S.1
  • 29
    • 33644874235 scopus 로고    scopus 로고
    • The integration of macromolecular diffraction data
    • Leslie A (2006) The integration of macromolecular diffraction data. Acta Crystallogr D 62:48-57.
    • (2006) Acta Crystallogr D , vol.62 , pp. 48-57
    • Leslie, A.1
  • 30
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy AJ, et al. (2007) Phaser crystallographic software. J Appl Crystallogr 40:658-674.
    • (2007) J Appl Crystallogr , vol.40 , pp. 658-674
    • McCoy, A.J.1
  • 31
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collarorative Computational Project Number 4
    • Collarorative Computational Project Number 4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr D 50:760-763.
    • (1994) Acta Crystallogr D , vol.50 , pp. 760-763
  • 32
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P. Cowtan K (2004) Coot: Model-building tools for molecular graphics. Acta Crystallogr D 60:2126-2132.
    • (2004) Acta Crystallogr D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.