Models of the three-dimensional structures of echidna, horse, and pigeon lysozymes

Calcium-binding lysozymes and their relationship with α-lactalbumins

K. Ravi Acharya, David I. Stuart, David C. Phillips, Hugh A. McKenzie, Carmel G. Teahan

Research output: Contribution to journalArticle

Abstract

Similarities in amino acid sequences, three-dimensional structures, and the exon-intron patterns of their genes have indicated that c-type lysozymes and α-lactalbumins are homologous proteins, i.e., descended by divergent evolution from a common ancestor. Like the α-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 α-lactalbumins, have been built. The several structures have been compared and their relationships discussed.

Original languageEnglish
Pages (from-to)569-584
Number of pages16
JournalJournal of Protein Chemistry
Volume13
Issue number6
DOIs
Publication statusPublished - 1 Aug 1994

Keywords

  • α-lactalbumin
  • Calcium-binding lysozyme
  • evolution
  • three-dimensional structure

ASJC Scopus subject areas

  • Biochemistry

Cite this

Models of the three-dimensional structures of echidna, horse, and pigeon lysozymes : Calcium-binding lysozymes and their relationship with α-lactalbumins. / Acharya, K. Ravi; Stuart, David I.; Phillips, David C.; McKenzie, Hugh A.; Teahan, Carmel G.

In: Journal of Protein Chemistry, Vol. 13, No. 6, 01.08.1994, p. 569-584.

Research output: Contribution to journalArticle

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