pubmed-article:18430721 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:18430721 | lifeskim:mentions | umls-concept:C0001511 | lld:lifeskim |
pubmed-article:18430721 | lifeskim:mentions | umls-concept:C0021027 | lld:lifeskim |
pubmed-article:18430721 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
pubmed-article:18430721 | lifeskim:mentions | umls-concept:C2599702 | lld:lifeskim |
pubmed-article:18430721 | lifeskim:mentions | umls-concept:C1883220 | lld:lifeskim |
pubmed-article:18430721 | pubmed:issue | 26 | lld:pubmed |
pubmed-article:18430721 | pubmed:dateCreated | 2008-6-23 | lld:pubmed |
pubmed-article:18430721 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18430721 | pubmed:abstractText | 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 2.8A 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/hetero-oligomerizations and should represent a general architecture of other CD147 family members. | lld:pubmed |
pubmed-article:18430721 | pubmed:language | eng | lld:pubmed |
pubmed-article:18430721 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18430721 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:18430721 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:18430721 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18430721 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:18430721 | pubmed:month | Jun | lld:pubmed |
pubmed-article:18430721 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:18430721 | pubmed:author | pubmed-author:VyasSS | lld:pubmed |
pubmed-article:18430721 | pubmed:author | pubmed-author:LykeSS | lld:pubmed |
pubmed-article:18430721 | pubmed:author | pubmed-author:ZhangJianJ | lld:pubmed |
pubmed-article:18430721 | pubmed:author | pubmed-author:JiangHualiang... | lld:pubmed |
pubmed-article:18430721 | pubmed:author | pubmed-author:ZhangZhengZ | lld:pubmed |
pubmed-article:18430721 | pubmed:author | pubmed-author:ChenZhi-NanZN | lld:pubmed |
pubmed-article:18430721 | pubmed:author | pubmed-author:ShenXuX | lld:pubmed |
pubmed-article:18430721 | pubmed:author | pubmed-author:ZhuPingP | lld:pubmed |
pubmed-article:18430721 | pubmed:author | pubmed-author:YuXiao-LingXL | lld:pubmed |
pubmed-article:18430721 | pubmed:author | pubmed-author:ZhongWei-DeWD | lld:pubmed |
pubmed-article:18430721 | pubmed:author | pubmed-author:DingJian-Ping... | lld:pubmed |
pubmed-article:18430721 | pubmed:author | pubmed-author:YangXiang-Min... | lld:pubmed |
pubmed-article:18430721 | pubmed:author | pubmed-author:HuTiancenT | lld:pubmed |
pubmed-article:18430721 | pubmed:author | pubmed-author:DuJia-MuJM | lld:pubmed |
pubmed-article:18430721 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:18430721 | pubmed:day | 27 | lld:pubmed |
pubmed-article:18430721 | pubmed:volume | 283 | lld:pubmed |
pubmed-article:18430721 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:18430721 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:18430721 | pubmed:pagination | 18056-65 | lld:pubmed |
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pubmed-article:18430721 | pubmed:meshHeading | pubmed-meshheading:18430721... | lld:pubmed |
pubmed-article:18430721 | pubmed:year | 2008 | lld:pubmed |
pubmed-article:18430721 | pubmed:articleTitle | Crystal structure of HAb18G/CD147: implications for immunoglobulin superfamily homophilic adhesion. | lld:pubmed |
pubmed-article:18430721 | pubmed:affiliation | Cell Engineering Research Center & Department of Cell Biology, State Key Laboratory of Cancer Biology, Xijing Hospital, the Fourth Military Medical University, Xi'an, China. | lld:pubmed |
pubmed-article:18430721 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:18430721 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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