This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1ala
From Proteopedia
|
STRUCTURE OF CHICKEN ANNEXIN V AT 2.25-ANGSTROMS RESOLUTION
Overview
The crystal structure of chicken annexin V has been solved by molecular, replacement and refined at 2.25 A. The final R factor is 19.7% with good, geometry. The chicken annexin V structure is very similar to the human, annexin V structure, with four similar domains each containing five, helices. The structure includes three calcium ions in domains I, II, and, IV, each bound by the characteristic K-G-X-G-T-(38 residues)-D/E motif. In, view of the structural similarity between human and chicken annexin V, we, suggest that they have a common vital function which developed early in, evolutionary history.
About this Structure
1ALA is a Single protein structure of sequence from Gallus gallus with CA as ligand. Full crystallographic information is available from OCA.
Reference
Structure of chicken annexin V at 2.25-A resolution., Bewley MC, Boustead CM, Walker JH, Waller DA, Huber R, Biochemistry. 1993 Apr 20;32(15):3923-9. PMID:8471604
Page seeded by OCA on Tue Nov 20 10:56:32 2007
