Autor: |
Roterman, Irena, Stapor, Katarzyna, Dułak, Dawid, Konieczny, Leszek |
Předmět: |
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Zdroj: |
FEBS Open Bio; Dec2024, Vol. 14 Issue 12, p2006-2025, 20p |
Abstrakt: |
The domain‐swapping mechanism involves the exchange of structural elements within a secondary or supersecondary structure between two (or more) proteins. The present paper proposes to interpret the domain‐swapping mechanism using a model that assesses the structure of proteins (and complexes) based on building the structure of a common hydrophobic core in a micelle‐like arrangement (a central hydrophobic core with a polar shell in contact with polar water), which has a considerable impact on the stabilisation of the domain structure built by domain swapping. Domains with a hydrophobicity system that is incompatible with the micelle‐like structure have also been identified. This incompatibility is the form of structural codes related to biological function. [ABSTRACT FROM AUTHOR] |
Databáze: |
Complementary Index |
Externí odkaz: |
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