Models of the three-dimensional structures of echidna, horse, and pigeon lysozymes: calcium-binding lysozymes and their relationship with alpha-lactalbumins.
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.
Department of Biochemistry, University of Bath, England.
K R
KR
Acharya
D I
DI
Stuart
D C
DC
Phillips
H A
HA
McKenzie
C G
CG
Teahan
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D005075:Biological Evolution; D002118:Calcium / Q000378:metabolism*; D010856:Columbidae; D004527:Egg Proteins / Q000737:chemistry; D006736:Horses; D007527:Isoenzymes / Q000737:chemistry*; D007768:Lactalbumin / Q000737:chemistry*; D008894:Milk Proteins / Q000737:chemistry; D008969:Molecular Sequence Data; D009113:Muramidase / Q000737:chemistry*; D011487:Protein Conformation; D004442:Tachyglossidae
D004527:Egg Proteins; D007527:Isoenzymes; D008894:Milk Proteins; D007768:Lactalbumin; D009113:Muramidase; D002118:Calcium