Grafting a short chameleon sequence from αB crystallin into a β‐sheet scaffold protein
| العنوان: | Grafting a short chameleon sequence from αB crystallin into a β‐sheet scaffold protein |
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| المؤلفون: | Wataru Fujiwara, Koki Makabe, Hideki Fujiwara, Yuki Hori |
| المصدر: | Proteins: Structure, Function, and Bioinformatics. 87:416-424 |
| بيانات النشر: | Wiley, 2019. |
| سنة النشر: | 2019 |
| مصطلحات موضوعية: | Models, Molecular, Scaffold protein, Amyloid, Protein Conformation, Beta sheet, Peptide, Sequence (biology), Crystallography, X-Ray, Biochemistry, Oligomer, Protein Structure, Secondary, 03 medical and health sciences, Amyloid disease, chemistry.chemical_compound, Nuclear Matrix-Associated Proteins, Structural Biology, Amino Acid Sequence, Molecular Biology, Peptide sequence, 030304 developmental biology, chemistry.chemical_classification, 0303 health sciences, Amyloid beta-Peptides, 030302 biochemistry & molecular biology, alpha-Crystallin B Chain, chemistry, Biophysics, Protein Conformation, beta-Strand |
| الوصف: | Many protein and peptide sequences are self-assembled into β-sheet-rich fibrous structures called amyloids. Their atomic details provide insights into fundamental knowledge related to amyloid diseases. To study the detailed structure of the amyloid, we have developed a model system that mimics the self-assembling process of the amyloid within a water-soluble protein, termed peptide self-assembly mimic (PSAM). PSAM enables capturing of a peptide sequence within a water-soluble protein, thus making structural and energetics-related studies possible. In this work, we extend our PSAM approach to a naturally occurring chameleon sequence from αB crystallin. We chose "Val-Leu-Gly-Asp-Val (VLGDV)", a five amino-acid sequence, which forms a β-turn in the native structure and a β-barrel in the amyloid oligomer cylindrin, as a grafting sequence to the PSAM scaffold. The crystal structure revealed that the sequence grafting induced β-sheet bending at the grafted site. We further investigated the role of the central glycine residue and found that its role in the β-sheet bending is dependent on the neighboring residues. The ability of PSAM to observe the structural alterations induced by the grafted sequence provides an opportunity to evaluate the structural impact of a sequence from the peptide self-assembly. |
| تدمد: | 1097-0134 0887-3585 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6c4a32a11b1eaf6335d45ba07af07743Test https://doi.org/10.1002/prot.25663Test |
| حقوق: | CLOSED |
| رقم الانضمام: | edsair.doi.dedup.....6c4a32a11b1eaf6335d45ba07af07743 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 10970134 08873585 |
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