Predicted structure for the calcium-dependent membrane-binding proteins p35, p36 and p32
- 1 June 1987
- journal article
- research article
- Published by Oxford University Press (OUP) in Protein Engineering, Design and Selection
- Vol. 1 (3) , 183-187
- https://doi.org/10.1093/protein/1.3.183
Abstract
A new family of proteins (annexins) that bind to membranes at micromolar free Ca2+ has been recognized. Its members include an EGF-receptor kinase substrate (p35) a retroviral tyrosine kinase substrate (p36), the liver protein endonexin (p32) and an electric ray protein, calelectrin. Each protein contains four sequence repeats with a further 2-fold Internal homology. Using the predicted secondary structure and pat tern of conserved hydrophobic residues in each repeat, we have built a three-dimensional model that is largely isostruc tural with the known molecular conformation of bovine In testinal calcium-binding protein. The final (energy-refined) model had a core formed from the conserved hydrophobic residues. It differed from ICaBP principally in the length of the two Ca2+ loops with only one loop being able to bind. The model suuggest a mechanism for interaction of these new Ca2+ proteins with phospholipid bilayers.This publication has 16 references indexed in Scilit:
- Amino-terminal sequence of p36 and associated p10: identification of the site of tyrosine phosphorylation and homology with S-100.Proceedings of the National Academy of Sciences, 1985
- Isolation of mammalian calelectrins: a new class of ubiquitous calcium(2+)-regulated proteinsBiochemistry, 1984
- Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical featuresBiopolymers, 1983
- Correlation of the Amino Acid Composition of a Protein to Its Structural and Biological Characters1The Journal of Biochemistry, 1982
- Active site and catalytic mechanism of phospholipase A2Nature, 1981
- Methylation of histidine-48 in pancreatic phospholipase A2. Role of histidine and calcium ion in the catalytic mechanismBiochemistry, 1980
- Spectroscopic studies on the binding of divalent cations to porcine intestinal calcium-binding proteinCanadian Journal of Biochemistry, 1978
- Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteinsJournal of Molecular Biology, 1978
- An assessment of protein secondary structure prediction methods based on amino acid sequenceBiochimica et Biophysica Acta (BBA) - Protein Structure, 1976
- Structural patterns in globular proteinsNature, 1976