α-lactalbumin possesses a distinct zinc binding site
| Autor: | Ren, J., Stuart, D. I., K. Ravi Acharya |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 1993 |
| Předmět: | |
| Zdroj: | Scopus-Elsevier |
| ISSN: | 0021-9258 |
| Popis: | It has been proposed that the binding of Zn2+ to α-lactalbumin switches the conformation to one akin to a state intermediate in the folding of the protein. However, the high resolution x-ray crystal structure of human α-lactalbumin-Zn2+ complex at 1.7-Å resolution (pH 7.6) does not reveal any significant change in conformation from the native state. The Zn2+ ion binds specifically in the "cleft" of α-lactalbumin (the region which forms the active site of the homologous protein lysozyme). This may suggest a possible role for Zn2+ binding in lactose synthase complex. The coordination of the Zn2+ ion involves a symmetry-related molecule in the crystal, the crystal contacts being stabilized by a SO42- ion bound at the interface between three molecules. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|