X-ray and primary structure of horse serum albumin (Equus caballus) at 0.27-nm resolution.
Abstract: 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.
Publication Date: 1993-07-01 PubMed ID: 8344282DOI: 10.1111/j.1432-1033.1993.tb18024.xGoogle Scholar: Lookup
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- Journal Article
- Research Support
- U.S. Gov't
- Non-P.H.S.
Summary
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The research uncovers the primary structure and three-dimensional structure of equine serum albumin, an important protein found in horse serum, at a microscopic resolution of 0.27 nanometers.
Amino-acid Sequence Determination
- The sequence of amino acids in equine serum albumin was deciphered using cDNA found in the liver of a horse.
- By comparing this primary structure with the serum albumin of humans and cows, it was found to have 76.1% and 73.9% sequence identity, respectively. This means there’s a significant similarity in the primary structure of these proteins cross-species.
Three-Dimensional Structure Exploration
- The molecule’s three-dimensional (3D) structure was figured out crystallographically, that is, by studying the arrangement of atoms within the crystal structure of the protein.
- The molecular replacement method was used for this purpose, where the previously known structure of human serum albumin was taken as a starting point.
- This structure is preserved across the proteins, as indicated by the alignment of the alpha-carbons in the amino acid chains of horse and human serum albumin, with a root-mean-square difference of 0.201 nm. This value is a measure of deviation between two datasets or structures.
Binding Affinity Analysis
- The capability of equine serum albumin to bond with 2,3,5-triiodobenzoic acid, a compound utilized as a reference in molecular binding studies, was also assessed.
- Binding constants (Ka) for horse and human serum albumin were found to be about 10(4) M-1 and 10(5) M-1, respectively, suggesting a stronger affinity of this acid for the human version of the protein.
Investigating Specific Binding Sites
- X-ray crystallographic analysis revealed two identical binding points for 2,3,5-triiodobenzoic acid in equine serum albumin that were the same as those found in human serum albumin.
- These binding points are located in distinct subdomains known as IIA and IIIA.
- The investigators also discussed additional details and comparisons of the binding chemistry involved.
Cite This Article
APA
Ho JX, Holowachuk EW, Norton EJ, Twigg PD, Carter DC.
(1993).
X-ray and primary structure of horse serum albumin (Equus caballus) at 0.27-nm resolution.
Eur J Biochem, 215(1), 205-212.
https://doi.org/10.1111/j.1432-1033.1993.tb18024.x Publication
Researcher Affiliations
- NASA, Marshall Space Flight Center, Huntsville, AL 35812.
MeSH Terms
- Amino Acid Sequence
- Animals
- Base Sequence
- Binding Sites
- Computer Graphics
- Horses
- Molecular Sequence Data
- Protein Structure, Tertiary
- Serum Albumin / chemistry
- X-Ray Diffraction
Citations
This article has been cited 18 times.- Victor S, Binnmyr J, Lampa E, Rask-Andersen A, Elfman L. Levels of horse allergen Equ c 4 in dander and saliva from ten horse breeds.. Clin Exp Allergy 2019 May;49(5):701-711.
- El-Fakharany EM, Abu-Serie MM, Litus EA, Permyakov SE, Permyakov EA, Uversky VN, Redwan EM. The Use of Human, Bovine, and Camel Milk Albumins in Anticancer Complexes with Oleic Acid.. Protein J 2018 Jun;37(3):203-215.
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