DC Field | Value | Language |
---|---|---|
dc.contributor.author | An, Hyun-Jung | ko |
dc.contributor.author | Kim, Young-Jin | ko |
dc.contributor.author | Song, Dong-Hyun | ko |
dc.contributor.author | Park, Beom-Seok | ko |
dc.contributor.author | Kim, Ho-Min | ko |
dc.contributor.author | Lee, Ju-Dong | ko |
dc.contributor.author | Paik, Sang-Gi | ko |
dc.contributor.author | Lee, Jie-Oh | ko |
dc.contributor.author | Lee, Hay-Young | ko |
dc.date.accessioned | 2013-03-09T07:09:56Z | - |
dc.date.available | 2013-03-09T07:09:56Z | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.issued | 2011-04 | - |
dc.identifier.citation | JOURNAL OF BIOLOGICAL CHEMISTRY, v.286, no.13, pp.11226 - 11235 | - |
dc.identifier.issn | 0021-9258 | - |
dc.identifier.uri | http://hdl.handle.net/10203/95679 | - |
dc.description.abstract | CD40 is a tumor necrosis factor receptor (TNFR) family protein that plays an important role in B cell development. CD154/CD40L is the physiological ligand of CD40. We have determined the crystal structure of the CD40-CD154 complex at 3.5 angstrom resolution. The binding site of CD40 is located in a crevice formed between two CD154 subunits. Charge complementarity plays a critical role in the CD40-CD154 interaction. Some of the missense mutations found in hereditary hyper-IgM syndrome can be mapped to the CD40-CD154 interface. The CD40 interaction area of one of the CD154 subunits is twice as large as that of the other subunit forming the binding crevice. This is because cysteine-rich domain 3 (CRD3) of CD40 has a disulfide bridge in an unusual position that alters the direction of the ladder-like structure of CD40. The Ser(132) loop of CD154 is not involved in CD40 binding but its substitution significantly reduces p38- and ERK-dependent signaling by CD40, whereas JNK-dependent signaling is not affected. These findings suggest that ligand-induced di- or trimerization is necessary but not sufficient for complete activation of CD40. | - |
dc.language | English | - |
dc.publisher | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | - |
dc.subject | HUMAN CD40 LIGAND | - |
dc.subject | X-LINKED IMMUNODEFICIENCY | - |
dc.subject | HYPER-IGM SYNDROME | - |
dc.subject | CRYSTAL-STRUCTURE | - |
dc.subject | MOLECULAR-MODELS | - |
dc.subject | FACTORS TRAFS | - |
dc.subject | BINDING | - |
dc.subject | DOMAIN | - |
dc.subject | CELLS | - |
dc.subject | GP39 | - |
dc.title | Crystallographic and Mutational Analysis of the CD40-CD154 Complex and Its Implications for Receptor Activation | - |
dc.type | Article | - |
dc.identifier.wosid | 000288797100034 | - |
dc.identifier.scopusid | 2-s2.0-79953229244 | - |
dc.type.rims | ART | - |
dc.citation.volume | 286 | - |
dc.citation.issue | 13 | - |
dc.citation.beginningpage | 11226 | - |
dc.citation.endingpage | 11235 | - |
dc.citation.publicationname | JOURNAL OF BIOLOGICAL CHEMISTRY | - |
dc.embargo.liftdate | 9999-12-31 | - |
dc.embargo.terms | 9999-12-31 | - |
dc.contributor.localauthor | Kim, Ho-Min | - |
dc.contributor.localauthor | Lee, Jie-Oh | - |
dc.contributor.nonIdAuthor | An, Hyun-Jung | - |
dc.contributor.nonIdAuthor | Paik, Sang-Gi | - |
dc.contributor.nonIdAuthor | Lee, Hay-Young | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordPlus | HUMAN CD40 LIGAND | - |
dc.subject.keywordPlus | X-LINKED IMMUNODEFICIENCY | - |
dc.subject.keywordPlus | HYPER-IGM SYNDROME | - |
dc.subject.keywordPlus | CRYSTAL-STRUCTURE | - |
dc.subject.keywordPlus | MOLECULAR-MODELS | - |
dc.subject.keywordPlus | FACTORS TRAFS | - |
dc.subject.keywordPlus | BINDING | - |
dc.subject.keywordPlus | DOMAIN | - |
dc.subject.keywordPlus | CELLS | - |
dc.subject.keywordPlus | GP39 | - |
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