6PLH

FAB fragment complexed with C-mannosylated tryptophan peptide

6PLH の概要

• エントリーDOI: 10.2210/pdb6plh/pdb
• 分子名称: Fab 5G12 light chain, Fab 5G12 heavy chain, Interleukin-21 receptor, ... (6 entities in total)
• 機能のキーワード: c-mannosylation, fab-fragment, immune system
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 52602.31

構造登録者

John, A.,Jarva, M.A.,Goddard-Borger, E.D. (登録日: 2019-06-30, 公開日: 2020-07-08, 最終更新日: 2024-11-20)

主引用文献

John, A.,Jarva, M.A.,Shah, S.,Mao, R.,Chappaz, S.,Birkinshaw, R.W.,Czabotar, P.E.,Lo, A.W.,Scott, N.E.,Goddard-Borger, E.D.
Yeast- and antibody-based tools for studying tryptophan C-mannosylation.
Nat.Chem.Biol., 17:428-437, 2021

PubMed Abstract: Tryptophan C-mannosylation is an unusual co-translational protein modification performed by metazoans and apicomplexan protists. The prevalence and biological functions of this modification are poorly understood, with progress in the field hampered by a dearth of convenient tools for installing and detecting the modification. Here, we engineer a yeast system to produce a diverse array of proteins with and without tryptophan C-mannosylation and interrogate the modification's influence on protein stability and function. This system also enabled mutagenesis studies to identify residues of the glycosyltransferase and its protein substrates that are crucial for catalysis. The collection of modified proteins accrued during this work facilitated the generation and thorough characterization of monoclonal antibodies against tryptophan C-mannosylation. These antibodies empowered proteomic analyses of the brain C-glycome by enriching for peptides possessing tryptophan C-mannosylation. This study revealed many new modification sites on proteins throughout the secretory pathway with both conventional and non-canonical consensus sequences.

PubMed: 33542533
DOI: 10.1038/s41589-020-00727-w

実験手法

X-RAY DIFFRACTION (1.6 Å)