Download MendeleyCrystal structure of the BAFF-BAFF-R complex and its implications for receptor activation
Kim, H.M., Yu, K.S., Lee, M.E., Shin, D.R., Kim, Y.S., Paik, S.G., Yoo, O.J., Lee, H., Lee, J.-O.(2003) Nat Struct Biol 10: 342-348
- PubMed: 12715002
- DOI: https://doi.org/10.1038/nsb925
- Primary Citation of Related Structures:
4V46 - PubMed Abstract:
B-cell activating factor (BAFF) is a key regulator of B-lymphocyte development. Its biological role is mediated by the specific receptors BCMA, TACI 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 A. 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 TACI-BAFF complex suggests that both CDRs simultaneously interact with the BAFF dimer in the virus-like cage.
Organizational Affiliation:
Department of Biological Science, Korea Advanced Institute of Science and Technology, Daejeon, Korea.
