5D4K

Crystal structure of the human polymeric Ig receptor (pIgR) ectodomain

5D4K の概要

• エントリーDOI: 10.2210/pdb5d4k/pdb
• 関連するPDBエントリー: 5F1S
• 分子名称: Polymeric immunoglobulin receptor, alpha-L-fucopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• 機能のキーワード: ig super family (igsf), polymeric ig-binding protein, mucosal immunity, secretory component, immune system
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 125412.21

構造登録者

Stadtmueller, B.M.,Bjorkman, P.J. (登録日: 2015-08-07, 公開日: 2016-03-16, 最終更新日: 2024-11-13)

主引用文献

Stadtmueller, B.M.,Huey-Tubman, K.E.,Lopez, C.J.,Yang, Z.,Hubbell, W.L.,Bjorkman, P.J.
The structure and dynamics of secretory component and its interactions with polymeric immunoglobulins.
Elife, 5:-, 2016

PubMed Abstract: As a first-line vertebrate immune defense, the polymeric immunoglobulin receptor (pIgR) transports polymeric IgA and IgM across epithelia to mucosal secretions, where the cleaved ectodomain (secretory component; SC) becomes a component of secretory antibodies, or when unliganded, binds and excludes bacteria. Here we report the 2.6Å crystal structure of unliganded human SC (hSC) and comparisons with a 1.7Å structure of teleost fish SC (tSC), an early pIgR ancestor. The hSC structure comprises five immunoglobulin-like domains (D1-D5) arranged as a triangle, with an interface between ligand-binding domains D1 and D5. Electron paramagnetic resonance measurements confirmed the D1-D5 interface in solution and revealed that it breaks upon ligand binding. Together with binding studies of mutant and chimeric SCs, which revealed domain contributions to secretory antibody formation, these results provide detailed models for SC structure, address pIgR evolution, and demonstrate that SC uses multiple conformations to protect mammals from pathogens.

PubMed: 26943617
DOI: 10.7554/eLife.10640

実験手法

X-RAY DIFFRACTION (2.599 Å)