6LFH
X-ray crystal structure of chemically synthesized human lysozyme
Summary for 6LFH
| Entry DOI | 10.2210/pdb6lfh/pdb |
| Descriptor | Lysozyme C, CHLORIDE ION, SODIUM ION, ... (4 entities in total) |
| Functional Keywords | human lysozyme, chemical protein synthesis, one-pot native chemical ligation, hydrolase |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 14979.39 |
| Authors | Kar, A.,Das, A.,Mandal, K. (deposition date: 2019-12-02, release date: 2020-07-08, Last modification date: 2023-11-22) |
| Primary citation | 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 Cited by 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: 32333711DOI: 10.1002/anie.202000491 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.46 Å) |
Structure validation
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