1ala: Difference between revisions
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'''STRUCTURE OF CHICKEN ANNEXIN V AT 2.25-ANGSTROMS RESOLUTION''' | '''STRUCTURE OF CHICKEN ANNEXIN V AT 2.25-ANGSTROMS RESOLUTION''' | ||
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[[Category: Huber, R.]] | [[Category: Huber, R.]] | ||
[[Category: Waller, D A.]] | [[Category: Waller, D A.]] | ||
[[Category: | [[Category: Calcium/phospholipid-binding protein]] | ||
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Revision as of 07:25, 2 May 2008
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. 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 Fri May 2 10:25:01 2008
