Literature DB >> 16029154

Structure and folding of potato type II proteinase inhibitors: circular permutation and intramolecular domain swapping.

Horst Joachim Schirra1, David J Craik.   

Abstract

Potato type II serine proteinase inhibitors are proteins that consist of multiple sequence repeats, and exhibit a multidomain structure. The structural domains are circular permutations of the repeat sequence, as a result of intramolecular domain swapping. Structural studies give indications for the origins of this folding behaviour, and the evolution of the inhibitor family.

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Year:  2005        PMID: 16029154     DOI: 10.2174/0929866054395266

Source DB:  PubMed          Journal:  Protein Pept Lett        ISSN: 0929-8665            Impact factor:   1.890


  2 in total

1.  Structural features of diverse Pin-II proteinase inhibitor genes from Capsicum annuum.

Authors:  Neha S Mahajan; Veena Dewangan; Purushottam R Lomate; Rakesh S Joshi; Manasi Mishra; Vidya S Gupta; Ashok P Giri
Journal:  Planta       Date:  2014-10-02       Impact factor: 4.116

2.  Tandem duplication, circular permutation, molecular adaptation: how Solanaceae resist pests via inhibitors.

Authors:  Lesheng Kong; Shoba Ranganathan
Journal:  BMC Bioinformatics       Date:  2008       Impact factor: 3.169

  2 in total

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