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| Autori principali: | , , , , , |
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| Natura: | Artículo Open Access |
| Pubblicazione: |
Wiley
2024
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| Soggetti: | |
| Accesso online: | https://onlinelibrary.wiley.com/doi/10.1002/prot.26698 |
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Sommario:
- Crystal structure of human Cep57 C‐terminal domain reveals the presence of leucine zipper and the potential microtubule binding region Sanskrita Sukla Dhayanitha Ranganathan Dhakshinamoorthy Arvind V. Ramesh Scott Lew Min Su Jayaraman Seetharaman Proteins: Structure, Function, and Bioinformatics Abstract Cep57, a vital centrosome‐associated protein, recruits essential regulatory enzymes for centriole duplication. Its dysfunction leads to anomalies, including reduced centrioles and mosaic‐variegated aneuploidy syndrome. Despite functional investigations, understanding structural aspects and their correlation with functions is partial till date. We present the structure of human Cep57 C‐terminal microtubule binding (MT‐BD) domain, revealing conserved motifs ensuring functional preservation across evolution. A leucine zipper, with an adjacent possible microtubule‐binding region, potentially forms a stabilizing scaffold for microtubule nucleation—accommodating pulling and tension from growing microtubules. This study highlights conserved structural features of Cep57 protein, compares them with other analogous proteins, and explores how protein function is maintained across diverse organisms. 10.1002/prot.26698 http://onlinelibrary.wiley.com/termsAndConditions#vor