4V46

Crystal structure of the BAFF-BAFF-R complex

これはPDB形式変換不可エントリーです。

4V46 の概要

• エントリーDOI: 10.2210/pdb4v46/pdb
• 分子名称: Tumor necrosis factor ligand superfamily member 13B, Tumor necrosis factor receptor superfamily member 13C, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: cytokine
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: 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
• タンパク質・核酸の鎖数: 120
• 化学式量合計: 1406707.46

構造登録者

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. (登録日: 2003-03-23, 公開日: 2014-07-09, 最終更新日: 2024-10-09)

主引用文献

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

実験手法

X-RAY DIFFRACTION (3.3 Å)