2LM3 : Structure of the rhesus monkey TRIM5alpha PRYSPRY domain

  • Nikolaos Biris (Contributor)
  • Andrei Tomashevski (Contributor)
  • Felipe Diaz-Griffero (Contributor)
  • Dmitri N Ivanov (Contributor)
  • Yang Yang (Contributor)
  • Alexander Bryan Taylor (Contributor)
  • Miao Guo (Contributor)
  • P. John Hart (Department of Veterans Affairs) (Contributor)



Experimental Technique/Method:SOLUTION NMR
Release Date:2012-08-08
Deposition Date:2011-11-21
Revision Date:2013-06-19
Molecular Weight:23361.43
Macromolecule Type:Protein
Residue Count:208
Atom Site Count:1630

Tripartite motif protein TRIM5α blocks retroviral replication after cell entry, and species-specific differences in its activity are determined by sequence variations within the C-terminal B30.2/PRYSPRY domain. Here we report a high-resolution structure of a TRIM5α PRYSPRY domain, the PRYSPRY of the rhesus monkey TRIM5α that potently restricts HIV infection, and identify features involved in its interaction with the HIV capsid. The extensive capsid-binding interface maps on the structurally divergent face of the protein formed by hypervariable loop segments, confirming that TRIM5α evolution is largely determined by its binding specificity. Interactions with the capsid are mediated by flexible variable loops via a mechanism that parallels antigen recognition by IgM antibodies, a similarity that may help explain some of the unusual functional properties of TRIM5α. Distinctive features of this pathogen-recognition interface, such as structural plasticity conferred by the mobile v1 segment and interaction with multiple epitopes, may allow restriction of divergent retroviruses and increase resistance to capsid mutations.
Date made available2012

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