Crystal structure of HAb18g/CD147 - Implications for immunoglobulin superfamily homophilic adhesion
Yu, Xiao-Ling2,3; Hu, Tiancen4; Du, Jia-Mu5; Ding, Jian-Ping5; Yang, Xiang-Min2,3; Zhang, Jian4; Yang, Bin2,3; Shen, Xu4; Zhang, Zheng2,3; Zhong, Wei-De6
刊名JOURNAL OF BIOLOGICAL CHEMISTRY
2008-06-27
卷号283期号:26页码:18056-18065
ISSN号0021-9258
DOI10.1074/jbc.M802694200
文献子类Article
英文摘要CD147, a member of the immunoglobulin superfamily (IgSF), plays fundamental roles in intercellular interactions in numerous pathological and physiological processes. Importantly, our previous studies have demonstrated that HAb18G/CD147 is a novel hepatocellular carcinoma (HCC)-associated antigen, and HAb18G/CD147 stimulates adjacent fibroblasts and HCC cells to produce elevated levels of several matrix metalloproteinases, facilitating invasion and metastasis of HCC cells. In addition, HAb18G/CD147 has also been shown to be a novel universal cancer biomarker for diagnosis and prognostic assessment of a wide range of cancers. However, the structural basis underlying the multifunctional character of CD147 remains unresolved. We report here the crystal structure of the extracellular portion of HAb18G/CD147 at 2.8 angstrom resolution. The structure comprises an N-terminal IgC2 domain and a C-terminal IgI domain, which are connected by a 5-residue flexible linker. This unique C2-I domain organization is distinct from those of other IgSF members. Four homophilic dimers exist in the crystal and adopt C2-C2 and C2-I dimerization rather than V-V dimerization commonly found in other IgSF members. This type of homophilic association thus presents a novel model for homophilic interaction between C2 domains of IgSF members. Moreover, the crystal structure of HAb18G/CD147 provides a good structural explanation for the established multifunction of CD147 mediated by homo/heterooligomerizations and should represent a general architecture of other CD147 family members.
WOS关键词MATRIX-METALLOPROTEINASE INDUCER ; CELL-SURFACE EXPRESSION ; MOLECULAR-DYNAMICS ; BINDING FRAGMENT ; SOLUBLE FORM ; RESOLUTION ; BASIGIN ; ANTIGEN ; CD147 ; RECOGNITION
WOS研究方向Biochemistry & Molecular Biology
语种英语
出版者AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
WOS记录号WOS:000256949200035
内容类型期刊论文
源URL[http://119.78.100.183/handle/2S10ELR8/272887]  
专题药物发现与设计中心
中科院受体结构与功能重点实验室
新药研究国家重点实验室
通讯作者Zhu, Ping
作者单位1.Fourth Mil Med Univ, Xijing Hosp, Dept Clin Immunol, Xian 710032, Peoples R China;
2.Fourth Mil Med Univ, State Key Lab Canc Biol, Dept Cell Biol, Xian 710032, Peoples R China;
3.Fourth Mil Med Univ, Cell Engn Res Ctr, Xian 710032, Peoples R China;
4.Shanghai Inst Mat Med, State Key Lab Drug Res, Drug Discovery & Design Ctr, Drug Discovery & Design Ctr, Shanghai 201203, Peoples R China;
5.Chinese Acad Sci, Shanghai Inst Biol Sci, Inst Biochem & Cell Biol, State Key Lab Mol Biol, Shanghai 200031, Peoples R China;
6.Guangzhou First Municipal Peoples Hosp, Guangzhou Med Coll, Guangzhou 510182, Peoples R China;
7.Chinese Peoples Liberat Army Gen Hosp, Beijing 100853, Peoples R China
推荐引用方式
GB/T 7714
Yu, Xiao-Ling,Hu, Tiancen,Du, Jia-Mu,et al. Crystal structure of HAb18g/CD147 - Implications for immunoglobulin superfamily homophilic adhesion[J]. JOURNAL OF BIOLOGICAL CHEMISTRY,2008,283(26):18056-18065.
APA Yu, Xiao-Ling.,Hu, Tiancen.,Du, Jia-Mu.,Ding, Jian-Ping.,Yang, Xiang-Min.,...&Chen, Zhi-Nan.(2008).Crystal structure of HAb18g/CD147 - Implications for immunoglobulin superfamily homophilic adhesion.JOURNAL OF BIOLOGICAL CHEMISTRY,283(26),18056-18065.
MLA Yu, Xiao-Ling,et al."Crystal structure of HAb18g/CD147 - Implications for immunoglobulin superfamily homophilic adhesion".JOURNAL OF BIOLOGICAL CHEMISTRY 283.26(2008):18056-18065.
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