The molecular structure of human erythropoietin.
The molecular structure of EPO has been discussed, and the gradual emergence of information about EPO has been reviewed. The importance of certain regions of the molecule and of glycosylation to EPO's structure and function are clear. Although its nucleotide and amino acid sequences are known, its tertiary structure remains elusive. Antipeptide antibody and mutagenesis studies have increased our ability to study structure/function and certain spatial relationships. Undoubtedly, additional information will continue to become available in this exciting area, providing a better understanding of the mechanisms behind EPO's central role in erythropoiesis.
Department of Medicine, State University of New York/Buffalo School of Medicine.
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Romanowski
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Sytkowski
D000595:Amino Acid Sequence; D000818:Animals; D000906:Antibodies / Q000097:blood; D002874:Chromosome Mapping; D004921:Erythropoietin / Q000737:chemistry* / Q000276:immunology / Q000502:physiology; D006801:Humans; D008969:Molecular Sequence Data; D016296:Mutagenesis / Q000502:physiology; D011994:Recombinant Proteins / Q000737:chemistry; D013045:Species Specificity; D013329:Structure-Activity Relationship
D000906:Antibodies; D011994:Recombinant Proteins; D004921:Erythropoietin