Segmentation strategy of de novo designed four-helical bundles expands protein oligomerization modalities for cell regulation
Povzetek
Protein–protein interactions govern most biological processes. New protein assemblies can be introduced through the fusion of selected proteins with di/oligomerization domains, which interact specifically with their partners but not with other cellular proteins. While four-helical bundle proteins (4HB) have typically been assembled from two segments, each comprising two helices, here we show that they can be efficiently segmented in various ways, expanding the number of combinations generated from a single 4HB. We implement a segmentation strategy of 4HB to design two-, three-, or four-chain combinations for the recruitment of multiple protein components. Different segmentations provide new insight into the role of individual helices for 4HB assembly. We evaluate 4HB segmentations for potential use in mammalian cells for the reconstitution of a protein reporter, transcriptional activation, and inducible 4HB assembly. Furthermore, the implementation of trimerization is demonstrated as a modular chimeric antigen receptor for the recognition of multiple cancer antigens.
Ključne besede
biokemija;proteini;beljakovine;antigenski receptorji;rakava obolenja;
Podatki
| Jezik: | Angleški jezik |
|---|---|
| Leto izida: | 2023 |
| Tipologija: | 1.01 - Izvirni znanstveni članek |
| Organizacija: | KI - Kemijski inštitut |
| Založnik: | Nature Publishing Group |
| UDK: | 577 |
| COBISS: |
150022147
|
| ISSN: | 2041-1723 |
| Št. ogledov: | 25 |
| Št. prenosov: | 5 |
| Ocena: | 0 (0 glasov) |
| Metapodatki: |
|
Ostali podatki
| Sekundarni jezik: | Slovenski jezik |
|---|---|
| Sekundarne ključne besede: | biokemija;proteini;beljakovine;antigenski receptorji;rakava obolenja; |
| Vrsta dela (COBISS): | Članek v reviji |
| Komentar vira: | Nasl. z nasl. zaslona; Opis vira z dne 21. 4. 2023; |
| Strani: | str. 1-12 |
| Letnik: | ǂVol. ǂ14 |
| Zvezek: | article no. 1995 |
| Čas izdaje: | 2023 |
| DOI: | 10.1038/s41467-023-37765-6 |
| ID: | 23267962 |
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