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It has been proposed that the binding of Zn2+ to alpha-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 alpha-lactalbumin-Zn2+ complex at 1.7-A 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 alpha-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

The Journal of biological chemistry

Publication Date

09/1993

Volume

268

Pages

19292 - 19298

Addresses

Oxford Centre for Molecular Sciences, New Chemistry Laboratory, United Kingdom.

Keywords

Humans, Zinc, Lactalbumin, X-Ray Diffraction, Binding Sites, Amino Acid Sequence, Protein Conformation, Protein Folding, Thermodynamics, Models, Molecular