메뉴 건너뛰기




Volumn 14, Issue 11, 2006, Pages 1611-1616

Complement and the Multifaceted Functions of VWA and Integrin I Domains

Author keywords

[No Author keywords available]

Indexed keywords

ANTHRAX TOXIN; COMPLEMENT COMPONENT C2; DNA; INTEGRIN; RNA; SERINE PROTEINASE; VON WILLEBRAND FACTOR;

EID: 33846213195     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2006.10.001     Document Type: Short Survey
Times cited : (80)

References (22)
  • 1
    • 1542603002 scopus 로고    scopus 로고
    • Crystal structure of the A domain from complement factor B reveals an integrin-like open conformation
    • Bhattacharya A.A., Lupher Jr. M.L., Staunton D.E., and Liddington R.C. Crystal structure of the A domain from complement factor B reveals an integrin-like open conformation. Structure 12 (2004) 371-378
    • (2004) Structure , vol.12 , pp. 371-378
    • Bhattacharya, A.A.1    Lupher Jr., M.L.2    Staunton, D.E.3    Liddington, R.C.4
  • 2
    • 0037136560 scopus 로고    scopus 로고
    • Structure of the Sec23/24-Sar1 prebudding complex of the COPII vesicle coat
    • Bi X., Corpina R.A., and Goldberg J. Structure of the Sec23/24-Sar1 prebudding complex of the COPII vesicle coat. Nature 419 (2002) 271-277
    • (2002) Nature , vol.419 , pp. 271-277
    • Bi, X.1    Corpina, R.A.2    Goldberg, J.3
  • 3
    • 0030770612 scopus 로고    scopus 로고
    • The von Willebrand factor A3 domain does not contain a metal ion-dependent adhesion site motif
    • Bienkowska J., Cruz M., Atiemo A., Handin R., and Liddington R. The von Willebrand factor A3 domain does not contain a metal ion-dependent adhesion site motif. J. Biol. Chem. 272 (1997) 25162-25167
    • (1997) J. Biol. Chem. , vol.272 , pp. 25162-25167
    • Bienkowska, J.1    Cruz, M.2    Atiemo, A.3    Handin, R.4    Liddington, R.5
  • 4
    • 2542480051 scopus 로고    scopus 로고
    • Crystal structure of the wild-type von Willebrand factor A1-glycoprotein Ibalpha complex reveals conformation differences with a complex bearing von Willebrand disease mutations
    • Dumas J.J., Kumar R., McDonagh T., Sullivan F., Stahl M.L., Somers W.S., and Mosyak L. Crystal structure of the wild-type von Willebrand factor A1-glycoprotein Ibalpha complex reveals conformation differences with a complex bearing von Willebrand disease mutations. J. Biol. Chem. 279 (2004) 23327-23334
    • (2004) J. Biol. Chem. , vol.279 , pp. 23327-23334
    • Dumas, J.J.1    Kumar, R.2    McDonagh, T.3    Sullivan, F.4    Stahl, M.L.5    Somers, W.S.6    Mosyak, L.7
  • 5
    • 0032562698 scopus 로고    scopus 로고
    • Crystal structure of the von Willebrand Factor A1 domain and implications for the binding of platelet glycoprotein Ib
    • Emsley J., Cruz M., Handin R., and Liddington R. Crystal structure of the von Willebrand Factor A1 domain and implications for the binding of platelet glycoprotein Ib. J. Biol. Chem. 273 (1998) 10396-10401
    • (1998) J. Biol. Chem. , vol.273 , pp. 10396-10401
    • Emsley, J.1    Cruz, M.2    Handin, R.3    Liddington, R.4
  • 8
    • 0025895079 scopus 로고
    • Site-directed mutagenesis of the region around Cys-241 of complement component C2. Evidence for a C4b binding site
    • Horiuchi T., Macon K.J., Engler J.A., and Volanakis J.E. Site-directed mutagenesis of the region around Cys-241 of complement component C2. Evidence for a C4b binding site. J. Immunol. 147 (1991) 584-589
    • (1991) J. Immunol. , vol.147 , pp. 584-589
    • Horiuchi, T.1    Macon, K.J.2    Engler, J.A.3    Volanakis, J.E.4
  • 11
    • 0034677208 scopus 로고    scopus 로고
    • New structural motifs on the chymotrypsin fold and their potential roles in complement factor B
    • Jing H., Xu Y., Carson M., Moore D., Macon K.J., Volanakis J.E., and Narayana S.V. New structural motifs on the chymotrypsin fold and their potential roles in complement factor B. EMBO J. 19 (2000) 164-173
    • (2000) EMBO J. , vol.19 , pp. 164-173
    • Jing, H.1    Xu, Y.2    Carson, M.3    Moore, D.4    Macon, K.J.5    Volanakis, J.E.6    Narayana, S.V.7
  • 12
    • 0019144945 scopus 로고
    • The human complement system: assembly of the classical pathway C3 convertase
    • Kerr M.A. The human complement system: assembly of the classical pathway C3 convertase. Biochem. J. 189 (1980) 173-181
    • (1980) Biochem. J. , vol.189 , pp. 173-181
    • Kerr, M.A.1
  • 13
    • 2342454381 scopus 로고    scopus 로고
    • Crystal structure of the von Willenbrand factor A domain of human capillary morphogenesis protein 2: an anthrax toxin receptor
    • Lacy D.B., Wigelsworth D.J., Scobie H.M., Young J.A.T., and Collier R.J. Crystal structure of the von Willenbrand factor A domain of human capillary morphogenesis protein 2: an anthrax toxin receptor. Proc. Natl. Acad. Sci. USA 101 (2004) 6367-6372
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 6367-6372
    • Lacy, D.B.1    Wigelsworth, D.J.2    Scobie, H.M.3    Young, J.A.T.4    Collier, R.J.5
  • 16
    • 1842816463 scopus 로고    scopus 로고
    • Structural analysis of engineered Bb fragment of complement factor B: insights into the activation mechanism of the alternative pathway C3-convertase
    • Ponnuraj K., Xu Y., Macon K., Moore D., Volanakis J.E., and Narayana S.V. Structural analysis of engineered Bb fragment of complement factor B: insights into the activation mechanism of the alternative pathway C3-convertase. Mol. Cell 14 (2004) 17-28
    • (2004) Mol. Cell , vol.14 , pp. 17-28
    • Ponnuraj, K.1    Xu, Y.2    Macon, K.3    Moore, D.4    Volanakis, J.E.5    Narayana, S.V.6
  • 18
    • 3542993051 scopus 로고    scopus 로고
    • Crystal structure of a complex between anthrax toxin and its host cell receptor
    • Santelli E., Bankston L.A., Leppla S.H., and Liddington R.C. Crystal structure of a complex between anthrax toxin and its host cell receptor. Nature 430 (2004) 905-908
    • (2004) Nature , vol.430 , pp. 905-908
    • Santelli, E.1    Bankston, L.A.2    Leppla, S.H.3    Liddington, R.C.4
  • 19
    • 0021351421 scopus 로고
    • MHC class III products: an electron microscopic study of the C3 convertases of human complement
    • Smith C.A., Vogel C.-W., and Müller-Eberhard H.J. MHC class III products: an electron microscopic study of the C3 convertases of human complement. J. Exp. Med. 159 (1984) 324-329
    • (1984) J. Exp. Med. , vol.159 , pp. 324-329
    • Smith, C.A.1    Vogel, C.-W.2    Müller-Eberhard, H.J.3
  • 20
    • 19344362237 scopus 로고    scopus 로고
    • Structural insights into RNA quality control: the Ro autoantigen binds misfolded RNAs via its central cavity
    • Stein A.J., Fuchs G., Fu C., Wolin S.L., and Reinisch K.M. Structural insights into RNA quality control: the Ro autoantigen binds misfolded RNAs via its central cavity. Cell 121 (2005) 529-539
    • (2005) Cell , vol.121 , pp. 529-539
    • Stein, A.J.1    Fuchs, G.2    Fu, C.3    Wolin, S.L.4    Reinisch, K.M.5
  • 21
    • 0030948650 scopus 로고    scopus 로고
    • Surface loops adjacent to the cation-binding site of the complement factor B von Willebrand factor type A module determine C3b binding specificity
    • Tuckwell D.S., Xu Y., Newham P., Humphries M.J., and Volanakis J.E. Surface loops adjacent to the cation-binding site of the complement factor B von Willebrand factor type A module determine C3b binding specificity. Biochemistry 36 (1997) 6605-6613
    • (1997) Biochemistry , vol.36 , pp. 6605-6613
    • Tuckwell, D.S.1    Xu, Y.2    Newham, P.3    Humphries, M.J.4    Volanakis, J.E.5
  • 22
    • 0035833552 scopus 로고    scopus 로고
    • Structure of the Ku heterodimer bound to DNA and its implications for double-strand break repair
    • Walker J.R., Corpina R.A., and Goldberg J. Structure of the Ku heterodimer bound to DNA and its implications for double-strand break repair. Nature 412 (2001) 607-614
    • (2001) Nature , vol.412 , pp. 607-614
    • Walker, J.R.1    Corpina, R.A.2    Goldberg, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.