6PLH
FAB fragment complexed with C-mannosylated tryptophan peptide
Summary for 6PLH
| Entry DOI | 10.2210/pdb6plh/pdb |
| Descriptor | Fab 5G12 light chain, Fab 5G12 heavy chain, Interleukin-21 receptor, ... (6 entities in total) |
| Functional Keywords | c-mannosylation, fab-fragment, immune system |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 3 |
| Total formula weight | 52602.31 |
| Authors | John, A.,Jarva, M.A.,Goddard-Borger, E.D. (deposition date: 2019-06-30, release date: 2020-07-08, Last modification date: 2024-11-20) |
| Primary citation | 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 Cited by 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: 33542533DOI: 10.1038/s41589-020-00727-w PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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