Conformational analysis of the GTP-binding protein MxA using limited proteolysis

Anjali Varne, Karthika Muthukumaraswamy, Shashidhar S. Jatiani, Rohit Mittal

Research output: Contribution to journalArticlepeer-review

6 Scopus citations


Guanosine triphosphate (GTP)-binding proteins are known to function as molecular switches that cycle between GTP-bound and guanosine diphosphate (GDP)-bound states. Switching is achieved by the fact that G-proteins in the GTP-bound conformation can interact with a certain set of effector molecules while they interact with a different set of partners in their GDP-bound conformation. The antiviral properties of the interferon-induced MxA protein are critically dependent on the ability of MxA to bind GTP. Using limited proteolysis we analyzed the conformations of the MxA protein under nucleotide-free, GDP-bound, and GTP-bound conditions. We find that whereas the conformations of nucleotide-free MxA and GDP-bound MxA are essentially similar, GTP-binding causes a dramatic change in the conformation of MxA.

Original languageEnglish
Pages (from-to)129-132
Number of pages4
JournalFEBS Letters
Issue number1-3
StatePublished - 10 Apr 2002
Externally publishedYes


  • G-protein
  • MxA
  • Nucleotide exchange
  • Proteolysis


Dive into the research topics of 'Conformational analysis of the GTP-binding protein MxA using limited proteolysis'. Together they form a unique fingerprint.

Cite this