Computer graphics modelling of human renin. Specificity, catalytic activity and intron-exon junctions

Bancinyane L. Sibanda, Tom Blundell, Peter M. Hobart, M. Fogliano, Jasjit S. Bindra, Beryl W. Dominy, John M. Chirgwin

Research output: Contribution to journalArticle

98 Scopus citations

Abstract

A model has been constructed using computer graphics for human renin based on the sequence derived from that of the gene and the 3-dimensional structure defined at high resolution for other homologous aspartic proteinases. Human renin can adopt a 3-dimensional structure close to that of other aspartic proteinases, in which amino acids corresponding to intron-exon junctions in the gene are at surface regions in the 3-dimensional structure. As expected, the essential catalytic residues are retained and the nearby residue 304 is alanine as in the mouse sequence, supporting the idea that Asp 304 of other aspartic proteinases may contribute to the low pH of their optimal activity. There are interesting differences at subsite S'3 which may contribute to the specificity of human renin. Certain residues at the surface of the enzyme adjacent to the active site cleft are unique to renins and may play a role in recognition and binding of angiotensinogen.

Original languageEnglish (US)
Pages (from-to)102-111
Number of pages10
JournalFEBS Letters
Volume174
Issue number1
DOIs
StatePublished - Aug 20 1984

Keywords

  • Computer graphics model
  • Enzyme specificity
  • Human renin
  • Intron-exon junction

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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