Abstract
Calcium performs a unique role in biology, achieving biological effects through highly specific interactions with and modulation of target proteins 1. It has been proposed that calcium-modulated proteins possess a characteristic, evolutionarily related, binding fold, known as the EF-hand 2. The high-resolution X-ray structure of α-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 α-lactalbumin). This study, at 1.7 Å resolution, represents one of the most accurate analyses of a calcium binding protein yet reported.
Original language | English |
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Pages (from-to) | 84-87 |
Number of pages | 4 |
Journal | Nature |
Volume | 324 |
Issue number | 6092 |
DOIs | |
Publication status | Published - 1 Dec 1986 |
ASJC Scopus subject areas
- General