Abstract
4 Interestingly, however, PerCR does not show the specific targeting when introduced into the cells with a protein transfection reagent. To resolve the structural basis for peroxisomal localization of PerCR, we have determined the crystal structure of PerCR at 1.5 A resolution [1]. The structure revealed that the C-terminal PTS1 of each subunit of PerCR was involved in intersubunit interactions and was buried in the interior of the tetrameric molecule. These data indicate that the monomeric form of PerCR whose C-terminal PTS1 is exposed will be recognized by the PTS1 receptor Pex5p in the cytosol and then, is targeted into the peroxisome and thereby forms tetramer. [1] Tanaka et al., Structure 16, 388-397 (2008).
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callMore From: Acta Crystallographica Section A Foundations of Crystallography
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
