DC Field | Value | Language |
---|---|---|
dc.contributor.author | Kim, Ho Min | - |
dc.contributor.author | Yu, Kyung Sook | - |
dc.contributor.author | Lee, Mi Eun | - |
dc.contributor.author | Shin, Dong Ryeol | - |
dc.contributor.author | Kim, Young Sang | - |
dc.contributor.author | Paik, Sang-Gi | - |
dc.contributor.author | Yoo, Ook Joon | - |
dc.contributor.author | Lee, Hayyoung | - |
dc.contributor.author | Lee, Jie-Oh | - |
dc.date.accessioned | 2009-09-24T07:20:20Z | - |
dc.date.available | 2009-09-24T07:20:20Z | - |
dc.date.issued | 2003-05 | - |
dc.identifier.citation | NATURE STRUCTURAL BIOLOGY, Vol.10, No.5, pp.342-348 | en |
dc.identifier.issn | 1072-8368 | - |
dc.identifier.uri | http://hdl.handle.net/10203/11495 | - |
dc.description.abstract | B-cell activating factor (BAFF) is a key regulator of B-lymphocyte development. Its biological role is mediated by the specific receptors BCMA, TACT and BAFF-R. We have determined the crystal structure of the extracellular domain of BAFF-R bound to BAFF at a resolution of 3.3 Angstrom. The cysteine-rich domain (CRD) of the BAFF-R extracellular domain adopts a beta-hairpin structure and binds to the virus-like BAFF cage in a 1:1 molar ratio. The conserved DxL motif of BAFF-R is located on the tip of the beta-turn and is indispensable in the binding of BAFF. The crystal structure shows that a unique dimeric contact occurs between the BAFF-R monomers in the virus-like cage complex. The extracellular domain of TACI contains two CRDs, both of which contain the DxL motif. Modeling of TACT-BAFF complex suggests that both CDRs simultaneously interact with the BAFF dimer in the virus-like cage. | en |
dc.description.sponsorship | We thank the staff of the Cornell High Energy Synchrotron Source (MacCHESS) and Spring-8 for help with data collection. This work was supported in part by the Molecular Medicine Research Group Program of the Ministry of Science (J.-O.L) and Technology and by a Korea Research Foundation Grant (H.L.). | en |
dc.language.iso | en_US | en |
dc.publisher | Nature Publishing Group | en |
dc.subject | NECROSIS-FACTOR RECEPTOR | en |
dc.subject | B-LYMPHOCYTE STIMULATOR | en |
dc.subject | T-CELL ACTIVATION | en |
dc.subject | TNF-RECEPTOR | en |
dc.subject | AUTOIMMUNE-DISEASE | en |
dc.subject | FACTOR FAMILY | en |
dc.subject | MEMBER | en |
dc.subject | TACI | en |
dc.subject | BLYS | en |
dc.subject | MICE | en |
dc.title | Crystal structure of the BAFF-BAFF-R complex and its implications for receptor activation | en |
dc.type | Article | en |
dc.identifier.doi | 10.1038/nsb925 | - |
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