4V46

Crystal structure of the BAFF-BAFF-R complex

This is a non-PDB format compatible entry.

Summary for 4V46

• Entry DOI: 10.2210/pdb4v46/pdb
• Descriptor: Tumor necrosis factor ligand superfamily member 13B, Tumor necrosis factor receptor superfamily member 13C, MAGNESIUM ION (3 entities in total)
• Functional Keywords: cytokine
• Biological source: Homo sapiens (human); More
• Cellular location: Cell membrane; Single-pass type II membrane protein. Tumor necrosis factor ligand superfamily member 13b, soluble form: Secreted: Q9Y275; Membrane ; Single-pass type III membrane protein : Q96RJ3
• Total number of polymer chains: 120
• Total formula weight: 1406707.46

Authors

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. (deposition date: 2003-03-23, release date: 2014-07-09, Last modification date: 2024-10-09)

Primary citation

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.
Crystal structure of the BAFF-BAFF-R complex and its implications for receptor activation
NAT.STRUCT.BIOL., 10:342-348, 2003

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.

PubMed: 12715002
DOI: 10.1038/nsb925

Experimental method

X-RAY DIFFRACTION (3.3 Å)