DC Field | Value | Language |
---|---|---|
dc.contributor.author | KIM, YOUNGJIN | - |
dc.date.accessioned | 2019-04-07T20:52:18Z | - |
dc.date.available | 2019-04-07T20:52:18Z | - |
dc.date.created | 2019-03-11 | - |
dc.date.issued | 2011-04-01 | - |
dc.identifier.issn | 0021-9258 | - |
dc.identifier.uri | https://oasis.postech.ac.kr/handle/2014.oak/96467 | - |
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 | ASBMB | - |
dc.relation.isPartOf | JOURNAL OF BIOLOGICAL CHEMISTRY | - |
dc.title | Crystallographic and mutational analysis of the CD40-CD154 complex and its implications for receptor activation | - |
dc.type | Article | - |
dc.identifier.doi | 10.1074/jbc.M110.208215 | - |
dc.type.rims | ART | - |
dc.identifier.bibliographicCitation | JOURNAL OF BIOLOGICAL CHEMISTRY, v.286, no.13, pp.11226 - 11235 | - |
dc.identifier.wosid | 000288797100034 | - |
dc.citation.endPage | 11235 | - |
dc.citation.number | 13 | - |
dc.citation.startPage | 11226 | - |
dc.citation.title | JOURNAL OF BIOLOGICAL CHEMISTRY | - |
dc.citation.volume | 286 | - |
dc.contributor.affiliatedAuthor | KIM, YOUNGJIN | - |
dc.identifier.scopusid | 2-s2.0-79953229244 | - |
dc.description.journalClass | 1 | - |
dc.description.journalClass | 1 | - |
dc.description.isOpenAccess | N | - |
dc.type.docType | 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 | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
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