Literature DB >> 2153583

Is the pseudo-dyad in retroviral proteinase monomers structural or evolutionary?

J K Rao1, A Wlodawer.   

Abstract

A pseudo-dyad was found to exist in the monomers of the crystal structures of the proteinases from Rous sarcoma virus and the human immunodeficiency virus. This dyad, also discovered earlier in pepsin-like aspartic proteinases and considered to be of probable evolutionary origin, has been shown to arise as a result of the topology and the folding of the proteinase monomers and may not therefore have much evolutionary significance.

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Year:  1990        PMID: 2153583     DOI: 10.1016/0014-5793(90)80103-p

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  2 in total

Review 1.  The early years of retroviral protease crystal structures.

Authors:  Maria Miller
Journal:  Biopolymers       Date:  2010       Impact factor: 2.505

2.  Structure of equine infectious anemia virus proteinase complexed with an inhibitor.

Authors:  A Gustchina; J Kervinen; D J Powell; A Zdanov; J Kay; A Wlodawer
Journal:  Protein Sci       Date:  1996-08       Impact factor: 6.725

  2 in total

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