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Calcium performs a unique role in biology, achieving biological effects through highly specific interactions with and modulation of target proteins. It has been proposed that calcium-modulated proteins possess a characteristic, evolutionarily related, binding fold, known as the EF-hand. The high-resolution X-ray structure of alpha-lactalbumin reveals a Ca2+ binding fold that resembles an EF-hand only superficially and presumably has no evolutionary relationship with it. However, there is clear homology with the corresponding loop in c-type lysozyme (the 'parent' molecule of alpha-lactalbumin). This study, at 1.7 A resolution, represents one of the most accurate analyses of a calcium binding protein yet reported.

Original publication

DOI

10.1038/324084a0

Type

Journal article

Journal

Nature

Publication Date

06/11/1986

Volume

324

Pages

84 - 87

Keywords

Binding Sites, Biological Evolution, Calcium-Binding Proteins, Lactalbumin, Models, Molecular, Muramidase, X-Ray Diffraction