Bacterial expression and preliminary crystallographic studies of a 149‐residue fragment of human Caprin‐1. Issue 3 (1st March 2015)

• Record Type: Journal Article
• Authors: Wu, Yuhong; Zhu, Jiang; Huang, Xiaolan; Du, Zhihua
• Is Part Of: Acta crystallographica. Volume 71:Issue 3(2015:Mar.)
• Page Start: 324
• Page End: 329
• Publication Date: 2015-03-01
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X15002642
• Languages: English
• ISSNs: 2053-230X

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>Caprin‐1 is an RNA‐binding protein which plays critical roles in several important biological processes, including cellular proliferation, the interferon‐mediated antiviral innate immune response, the maintenance of synaptic plasticity and the formation of RNA stress granules. Caprin‐1 has been implicated in the pathogenesis of several human diseases, including osteosarcoma, breast cancer, viral infections, hearing loss and neurodegenerative disorders. Despite the emerging biological and physiopathological significance of Caprin‐1, no structural information is available for this protein. Moreover, Caprin‐1 does not have sequence similarity to any other protein with a known structure. It is therefore expected that structural studies will play a particularly crucial role in revealing the functional mechanisms of Caprin‐1. Here, a protein fragment of human Caprin‐1 consisting of residues 112–260 was expressed, purified and crystallized. Native and Se‐SAD data sets were collected to resolutions to 2.05 and 2.65 Å, respectively, in different space groups.</p> </abstract>