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PMID: 24179 Published · ppublish English Comparative Study Journal Article

Structural evidence for gene duplication in the evolution of the acid proteases.

Nature ·Vol. 271 ·No. 5646 ·1978-02-16 ·Pages 618-21

Tang J, James MN, Hsu IN, Jenkins JA, Blundell TL

Abstract

X-ray studies of acid proteases indicate a bilobal structure with a well defined active site cleft. An intramolecular twofold symmetry axis relates two topologically similar domains and the active site residues. A possible mechanism for evolution by gene duplication, divergence and gene fusion is presented.

MeSH Terms
Amino Acid Sequence Binding Sites Biological Evolution Genes Hydrogen-Ion Concentration Peptide Hydrolases/genetics Protein Conformation
Chemicals
Peptide Hydrolases
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Tang J
James M N
Hsu I N
Jenkins J A
Blundell T L
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
DOI
10.1038/271618a0
Published
1978-02-16
Pages
618-21
Language
English
Region
England
NLM ID
0410462
Subset
IM
External Links
PubMed source DOI: 10.1038/271618a0 View journal details
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