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  • 标题:Molecular basis for complement recognition by integrin αXβ2
  • 本地全文:下载
  • 作者:Xing Chen ; Yamei Yu ; Li-Zhi Mi
  • 期刊名称:Proceedings of the National Academy of Sciences
  • 印刷版ISSN:0027-8424
  • 电子版ISSN:1091-6490
  • 出版年度:2012
  • 卷号:109
  • 期号:12
  • 页码:4586-4591
  • DOI:10.1073/pnas.1202051109
  • 语种:English
  • 出版社:The National Academy of Sciences of the United States of America
  • 摘要:Integrin X{beta}2 functions as complement receptor for iC3b and mediates recognition and phagocytosis of pathogens. We used negative-stain EM to examine the X{beta}2 interaction with iC3b. EM class averages of X{beta}2 in complex with iC3b define the binding sites on both the integrin and iC3b. iC3b contains C3c and thioester domain moieties linked by a long flexible linker. The binding site is on the key ring of the C3c moiety, at the interface between the MG3 and MG4 domains. Similar complexes are seen between X{beta}2 and the C3c fragment. X{beta}2 binds through the X I domain, on the face known to bear the metal ion-dependent adhesion site, at the opposite end of the I domain from its site of insertion in the {beta}-propeller domain.
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