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It has been proposed that the binding of Zn2+ to α-lactalbumin switches the conformational 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 SO4/2- ion bound at the interface between three molecules.

Type

Journal article

Journal

Journal of Biological Chemistry

Publication Date

01/01/1993

Volume

268

Pages

19292 - 19298