6LFH

X-ray crystal structure of chemically synthesized human lysozyme

6LFH の概要

• エントリーDOI: 10.2210/pdb6lfh/pdb
• 分子名称: Lysozyme C, CHLORIDE ION, SODIUM ION, ... (4 entities in total)
• 機能のキーワード: human lysozyme, chemical protein synthesis, one-pot native chemical ligation, hydrolase
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14979.39

構造登録者

Kar, A.,Das, A.,Mandal, K. (登録日: 2019-12-02, 公開日: 2020-07-08, 最終更新日: 2024-11-13)

主引用文献

Kar, A.,Mannuthodikayil, J.,Singh, S.,Biswas, A.,Dubey, P.,Das, A.,Mandal, K.
Efficient Chemical Protein Synthesis using Fmoc-Masked N-Terminal Cysteine in Peptide Thioester Segments.
Angew.Chem.Int.Ed.Engl., 59:14796-14801, 2020

PubMed Abstract: We report an operationally simple method to facilitate chemical protein synthesis by fully convergent and one-pot native chemical ligations utilizing the fluorenylmethyloxycarbonyl (Fmoc) moiety as an N-masking group of the N-terminal cysteine of the middle peptide thioester segment(s). The Fmoc group is stable to the harsh oxidative conditions frequently used to generate peptide thioesters from peptide hydrazide or o-aminoanilide. The ready availability of Fmoc-Cys(Trt)-OH, which is routinely used in Fmoc solid-phase peptide synthesis, where the Fmoc group is pre-installed on cysteine residue, minimizes additional steps required for the temporary protection of the N-terminal cysteinyl peptides. The Fmoc group is readily removed after ligation by short exposure (<7 min) to 20 % piperidine at pH 11 in aqueous conditions at room temperature. Subsequent native chemical ligation reactions can be performed in presence of piperidine in the same solution at pH 7.

PubMed: 32333711
DOI: 10.1002/anie.202000491

実験手法

X-RAY DIFFRACTION (1.46 Å)