X-ray and primary structure of horse serum albumin (Equus caballus) at 0.27-nm resolution
| Autor: | Elizabeth J. Norton, Daniel C. Carter, Eugene W. Holowachuk, Pamela D. Twigg, Joseph X. Ho |
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| Rok vydání: | 1993 |
| Předmět: |
Binding Sites
Base Sequence Molecular Sequence Data Protein primary structure Albumin Serum albumin Biology Human serum albumin Biochemistry Molecular biology Protein Structure Tertiary Protein structure X-Ray Diffraction Computer Graphics biology.protein medicine Animals Amino Acid Sequence Horses Binding site Bovine serum albumin Peptide sequence Serum Albumin medicine.drug |
| Zdroj: | European Journal of Biochemistry. 215:205-212 |
| ISSN: | 1432-1033 0014-2956 |
| Popis: | The amino-acid sequence and three-dimensional structure of equine serum albumin have been determined. The amino-acid sequence was deduced from cDNA isolated from equine liver. Comparisons of the primary structure of equine serum albumin with human serum albumin and bovine serum albumin reveal 76.1% and 73.9% sequence identity, respectively. The three-dimensional structure was determined crystallographically by the molecular-replacement method using molecular coordinates from the previously determined structure of human serum albumin, to a resolution of 0.27 nm. In accordance with the primary structure, the three-dimensional structures are highly conserved. There is a root-mean-square difference between alpha-carbons of the two structures of 0.201 nm. The association constants (Ka) for the binding of 2,3,5-triiodobenzoic acid were determined by ultrafiltration methods for equine and human serum albumins to be approximately 10(4) M-1 and 10(5) M-1, respectively. Crystallographic studies of equine serum albumin reveal two binding sites for 2,3,5-triiodobenzoic acid identical with those previously reported for human serum albumin which are located within subdomains in IIA and IIIA. Details and comparisons of the binding chemistry are discussed. |
| Databáze: | OpenAIRE |
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