α-lactalbumin possesses a distinct zinc binding site

Journal article

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.

Authors: Ren, J; Stuart, D; Acharya, K

• Journal: Journal of Biological Chemistry
• Volume: 268
• Issue: 26
• Pages: 19292-19298
• Publication date: 1993-09-15
• ISSN: 0021-9258
• Language: English