Crystal structure of the BAFF-BAFF-R complex and its implications for receptor activation

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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.
Description
의과학대학원
Publisher
NATURE PUBLISHING GROUP
Issue Date
2003-05
Language
ENG
Article Type
Article
Citation

NATURE STRUCTURAL BIOLOGY v.10 no.1072-8368 pp.342 - 348

ISSN
1072-8368
URI
http://hdl.handle.net/10203/85919
Appears in Collection
NE-Journal Papers(저널논문)
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