α-lactalbumin possesses a novel calcium binding loop

D. I. Stuart, K. R. Acharya, N. P.C. Walker, S. G. Smith, M. Lewis, D. C. Phillips

Research output: Contribution to journalArticle

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 languageEnglish
Pages (from-to)84-87
Number of pages4
JournalNature
Volume324
Issue number6092
DOIs
Publication statusPublished - 1 Dec 1986

ASJC Scopus subject areas

  • General

Cite this

Stuart, D. I., Acharya, K. R., Walker, N. P. C., Smith, S. G., Lewis, M., & Phillips, D. C. (1986). α-lactalbumin possesses a novel calcium binding loop. Nature, 324(6092), 84-87. https://doi.org/10.1038/324084a0