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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ala ConSurf]. | ||
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Revision as of 15:49, 8 February 2016
STRUCTURE OF CHICKEN ANNEXIN V AT 2.25-ANGSTROMS RESOLUTIONSTRUCTURE OF CHICKEN ANNEXIN V AT 2.25-ANGSTROMS RESOLUTION
Structural highlights
Function[ANXA5_CHICK] Collagen-binding protein. Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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