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Computer graphics modelling of human renin
Author(s) -
Sibanda Bancinyane L.,
Blundell Tom,
Hobart Peter M.,
Fogliano M.,
Bindra Jasjit S.,
Dominy Beryl W.,
Chirgwin John M.
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)81086-8
Subject(s) - graphics , computer science , computer graphics , computer graphics (images) , chemistry
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.