The conformation of calreticulin is influenced by the endoplasmic reticulum luminal environment

In order to understand the dynamics of the endoplasmic reticulum (ER) luminal environment, we investigated the role of Ca(2+), Zn(2+), and ATP on conformational changes of calreticulin. Purified calreticulin was digested with trypsin in the presence or absence of Ca(2+), Zn(2+), and ATP. At low Ca(2...

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Bibliographic Details
Published in:The Journal of biological chemistry 2000-09, Vol.275 (35), p.27177-27185
Main Authors: Corbett, E F, Michalak, K M, Oikawa, K, Johnson, S, Campbell, I D, Eggleton, P, Kay, C, Michalak, M
Format: Article
Language:English
Subjects:
Adenosine Triphosphate - metabolism
Amino Acid Sequence
Animals
Calcium - metabolism
Calcium-Binding Proteins - chemistry
Calcium-Binding Proteins - metabolism
Calreticulin
Endoplasmic Reticulum - chemistry
Endoplasmic Reticulum - metabolism
Molecular Sequence Data
Protein Binding
Protein Conformation
Rabbits
Recombinant Proteins - chemistry
Recombinant Proteins - metabolism
Ribonucleoproteins - chemistry
Ribonucleoproteins - metabolism
Structure-Activity Relationship
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Summary:In order to understand the dynamics of the endoplasmic reticulum (ER) luminal environment, we investigated the role of Ca(2+), Zn(2+), and ATP on conformational changes of calreticulin. Purified calreticulin was digested with trypsin in the presence or absence of Ca(2+), Zn(2+), and ATP. At low Ca(2+) concentration (
ISSN:0021-9258
DOI:10.1016/s0021-9258(19)61495-x