Article
Change in the N-terminal domain conformation of annexin I that correlates with liposome aggregation is impaired by Ser-27 to Glu mutation that mimics phosphorylation.
Biochimica et biophysica acta - 16 Apr 1996
Porte F, de Santa Barbara P, Phalipou S, Liautard J P, Widada J S
Abstract excerpt
Annexin I is a member of the annexin family of calcium-dependent membrane binding proteins. The core domain of these proteins is similar in all annexins but the N-terminal domain is specific for each member. This domain is thought to regulate annexin function through phosphorylation. In annexin I...
Topics
- Annexin A1
- Base Sequence
- Calcium
- Electrophoresis, Polyacrylamide Gel
- Liposomes
- Molecular Sequence Data
- Mutagenesis, Site-Directed
- Mutation
- Phosphorylation
- Protein Conformation
- Recombinant Proteins
- Serine
- Spectrometry, Fluorescence
- Trypsin
- Tryptophan