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.
Publisher
Nature Publishing Group
Issue Date
2003-05
Keywords

NECROSIS-FACTOR RECEPTOR; B-LYMPHOCYTE STIMULATOR; T-CELL ACTIVATION; TNF-RECEPTOR; AUTOIMMUNE-DISEASE; FACTOR FAMILY; MEMBER; TACI; BLYS; MICE

Citation

NATURE STRUCTURAL BIOLOGY, Vol.10, No.5, pp.342-348

ISSN
1072-8368
DOI
10.1038/nsb925
URI
http://hdl.handle.net/10203/11495
Appears in Collection
CH-Journal Papers(저널논문)

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