Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

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