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Home / Equine Research Bank / J Protein Chem / Models of the three-dimensional structures of echidna, horse...
Journal of protein chemistry1994; 13(6); 569-584; doi: 10.1007/BF01901539

Models of the three-dimensional structures of echidna, horse, and pigeon lysozymes: calcium-binding lysozymes and their relationship with alpha-lactalbumins.

Abstract: Similarities in amino acid sequences, three-dimensional structures, and the exon-intron patterns of their genes have indicated that c-type lysozymes and alpha-lactalbumins are homologous proteins, i.e., descended by divergent evolution from a common ancestor. Like the alpha-lactalbumins, echidna milk, horse milk, and pigeon eggwhite lysozymes all bind Ca(II). Models of their three-dimensional structures, based on their amino acid sequences and the known crystal structures of domestic hen eggwhite and human lysozymes and baboon and human alpha-lactalbumins, have been built. The several structures have been compared and their relationships discussed.
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Publication Date: 1994-08-01 PubMed ID: 7832986DOI: 10.1007/BF01901539Google Scholar: Lookup
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Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

The research investigates the three-dimensional structures of echidna, horse, and pigeon lysozymes, proteins that bind calcium, and their relationship with alpha-lactalbumins.

Objective of the Research

  • The goal of the study is to analyse and compare the three-dimensional structures of echidna, horse, and pigeon lysozymes, which are proteins known to bind calcium. Additionally, the research seeks to establish the relationships these structures have with alpha-lactalbumins, a group of proteins commonly found in milk.

Background and Significance

  • Previous studies have suggested that c-type lysozymes and alpha-lactalbumins, due to similarities in their amino acid sequences, three-dimensional structures, and the exon-intron patterns of their genes, are homologous proteins, meaning they’ve descended from a common ancestor through divergent evolution.
  • Alpha-lactalbumins are known to bind to calcium (Ca(II)). The mention of echidna milk, horse milk, and pigeon eggwhite lysozymes also binding to Ca(II) suggests some similarities between these lysozymes and alpha-lactalbumins.

Methodology and Results

  • The researchers built models of the three-dimensional structures of the lysozymes based on their amino acid sequences. The known crystal structures of domestic hen eggwhite and human lysozymes and baboon and human alpha-lactalbumins were used as a reference for building these models.
  • Comparative analysis was carried out on the models to determine their relationships. Through this comparison, the researchers were able to further establish the connections between these lysozymes and alpha-lactalbumins.

Conclusions and Implications

  • Though the abstract does not provide explicit findings or conclusions, the study can be inferred to have made progress in understanding the nature and relationships among these proteins, and thereby uncovering insights about protein evolution and calcium-binding functionality.
  • The research may contribute to the understanding of the proteins’ biological functions, which are not only important in evolutionary biology, but also in medical and biotechnological applications.

Cite This Article

APA
Acharya KR, Stuart DI, Phillips DC, McKenzie HA, Teahan CG. (1994). Models of the three-dimensional structures of echidna, horse, and pigeon lysozymes: calcium-binding lysozymes and their relationship with alpha-lactalbumins. J Protein Chem, 13(6), 569-584. https://doi.org/10.1007/BF01901539

Publication

Journal of protein chemistry
ISSN: 0277-8033
NlmUniqueID: 8217321
Country: United States
Language: English
Volume: 13
Issue: 6
Pages: 569-584

Researcher Affiliations

Acharya, K R
  • Department of Biochemistry, University of Bath, England.
Stuart, D I
    Phillips, D C
      McKenzie, H A
        Teahan, C G

          MeSH Terms

          • Amino Acid Sequence
          • Animals
          • Binding Sites
          • Biological Evolution
          • Calcium / metabolism
          • Columbidae
          • Egg Proteins / chemistry
          • Horses
          • Isoenzymes / chemistry
          • Lactalbumin / chemistry
          • Milk Proteins / chemistry
          • Molecular Sequence Data
          • Muramidase / chemistry
          • Protein Conformation
          • Tachyglossidae

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          Citations

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