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Corrigendum to “Properdin: New roles in pattern recognition and target clearance” [Mol. Immunol. 45 (16) (2008) 4048–4056]
Molecular Immunology 46 (2009) 1569
Contents lists available at ScienceDirect
Molecular Immunology journal homepage: www.elsevier.com/locate/molimm
Corrigendum
Corrigendum to “Properdin: New roles in pattern recognition and target clearance” [Mol. Immunol. 45 (16) (2008) 4048–4056] Claudia Kemper a , Dennis E. Hourcade b,∗ a b
MRC Centre for Transplantation, King’s College London, UK Department of Medicine, Division of Rheumatology, Washington University School of Medicine, St. Louis, MO, USA
The authors regret that in the above article, the recent analysis of Sun et al. (2004), that demonstrates that the amino-terminal region of the properdin monomer forms a seventh thrombospondin repeat, was inadvertently omitted. This point is of structural and evolutionary significance and could be of functional importance. Page 4049, Section 2 (Properdin and the alternative pathway) lines 33–34 should read: “Each subunit is composed of 7 globular domains that are homologous to the thrombospondin type 1 repeat (Nolan et al., 1991; Sun et al., 2004).” Page 4051, Section 5 (Properdin binds the GAG chains on surface proteoglycans) lines 9–10 should read: “Properdin is composed of 7 thrombospondin type 1 repeats (TSRs) (Nolan et al., 1991; Sun et al., 2004).” References Nolan, K.F., Schwaeble, W., Kaluz, S., Dierich, M.P., Reid, K.B., 1991. Molecular cloning of the cDNA coding for properdin, a positive regulator of the alternative pathway of human complement. Eur. J. Immunol. 21, 771–776. Sun, Z., Reid, K.B.M., Perkins, S.J., 2004. The dimeric and trimeric solution structures of the multidomain complement protein properdin by X-ray scattering, analytical ultracentrifugation and constrained modelling. J. Mol. Biol. 343, 1327–1343.
DOI of original article:10.1016/j.molimm.2008.06.034. ∗ Corresponding author. E-mail address: [email protected] (D.E. Hourcade). 0161-5890/$ – see front matter © 2009 Elsevier Ltd. All rights reserved. doi:10.1016/j.molimm.2009.02.001
Contents lists available at ScienceDirect
Molecular Immunology journal homepage: www.elsevier.com/locate/molimm
Corrigendum
Corrigendum to “Properdin: New roles in pattern recognition and target clearance” [Mol. Immunol. 45 (16) (2008) 4048–4056] Claudia Kemper a , Dennis E. Hourcade b,∗ a b
MRC Centre for Transplantation, King’s College London, UK Department of Medicine, Division of Rheumatology, Washington University School of Medicine, St. Louis, MO, USA
The authors regret that in the above article, the recent analysis of Sun et al. (2004), that demonstrates that the amino-terminal region of the properdin monomer forms a seventh thrombospondin repeat, was inadvertently omitted. This point is of structural and evolutionary significance and could be of functional importance. Page 4049, Section 2 (Properdin and the alternative pathway) lines 33–34 should read: “Each subunit is composed of 7 globular domains that are homologous to the thrombospondin type 1 repeat (Nolan et al., 1991; Sun et al., 2004).” Page 4051, Section 5 (Properdin binds the GAG chains on surface proteoglycans) lines 9–10 should read: “Properdin is composed of 7 thrombospondin type 1 repeats (TSRs) (Nolan et al., 1991; Sun et al., 2004).” References Nolan, K.F., Schwaeble, W., Kaluz, S., Dierich, M.P., Reid, K.B., 1991. Molecular cloning of the cDNA coding for properdin, a positive regulator of the alternative pathway of human complement. Eur. J. Immunol. 21, 771–776. Sun, Z., Reid, K.B.M., Perkins, S.J., 2004. The dimeric and trimeric solution structures of the multidomain complement protein properdin by X-ray scattering, analytical ultracentrifugation and constrained modelling. J. Mol. Biol. 343, 1327–1343.
DOI of original article:10.1016/j.molimm.2008.06.034. ∗ Corresponding author. E-mail address: [email protected] (D.E. Hourcade). 0161-5890/$ – see front matter © 2009 Elsevier Ltd. All rights reserved. doi:10.1016/j.molimm.2009.02.001