Source:http://linkedlifedata.com/resource/pubmed/id/18430721
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
26
|
pubmed:dateCreated |
2008-6-23
|
pubmed:databankReference | |
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.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Jun
|
pubmed:issn |
0021-9258
|
pubmed:author |
pubmed-author:ChenZhi-NanZN,
pubmed-author:DingJian-PingJP,
pubmed-author:DuJia-MuJM,
pubmed-author:HuTiancenT,
pubmed-author:JiangHualiangH,
pubmed-author:LykeSS,
pubmed-author:ShenXuX,
pubmed-author:VyasSS,
pubmed-author:YangXiang-MinXM,
pubmed-author:YuXiao-LingXL,
pubmed-author:ZhangJianJ,
pubmed-author:ZhangZhengZ,
pubmed-author:ZhongWei-DeWD,
pubmed-author:ZhuPingP
|
pubmed:issnType |
Print
|
pubmed:day |
27
|
pubmed:volume |
283
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
18056-65
|
pubmed:meshHeading |
pubmed-meshheading:18430721-Amino Acid Sequence,
pubmed-meshheading:18430721-Antigens, CD147,
pubmed-meshheading:18430721-Cell Line, Tumor,
pubmed-meshheading:18430721-Crystallography, X-Ray,
pubmed-meshheading:18430721-Dimerization,
pubmed-meshheading:18430721-Humans,
pubmed-meshheading:18430721-Immunoglobulins,
pubmed-meshheading:18430721-Models, Molecular,
pubmed-meshheading:18430721-Molecular Conformation,
pubmed-meshheading:18430721-Molecular Sequence Data,
pubmed-meshheading:18430721-Neoplasm Metastasis,
pubmed-meshheading:18430721-Protein Structure, Tertiary,
pubmed-meshheading:18430721-Sequence Homology, Amino Acid,
pubmed-meshheading:18430721-Thermodynamics,
pubmed-meshheading:18430721-Tumor Markers, Biological
|
pubmed:year |
2008
|
pubmed:articleTitle |
Crystal structure of HAb18G/CD147: implications for immunoglobulin superfamily homophilic adhesion.
|
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.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|