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Homology among acid proteases: comparison of crystal structures at 3A resolution of acid proteases from Rhizopus chinensis and Endothia parasitica.

Authors
  • Subramanian, E
  • Swan, I D
  • Liu, M
  • Davies, D R
  • Jenkins, J A
  • Tickle, I J
  • Blundell, T L
Type
Published Article
Journal
Proceedings of the National Academy of Sciences
Publisher
Proceedings of the National Academy of Sciences
Publication Date
Feb 01, 1977
Volume
74
Issue
2
Pages
556–559
Identifiers
PMID: 322132
Source
Medline
License
Unknown

Abstract

The molecular structures of two fungal acid proteases at 3 A resolution have been compared, and found to have similar secondary and tertiary folding. These enzymes are bilobal and have a pronounced cleft between the two lobes. This cleft has been identified as the active site region from inhibitor binding studies. The results of the comparison are discussed in terms of homology among the acid proteases in general.

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