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. 2019 Apr 25;34(2):135–161. doi: 10.1007/s12250-019-00114-3

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© The Author(s) 2019

Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.

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Fig. 4 — Structural composition of ORF57 protein. KSHV ORF57 contains two structurally and functionally distinct domains. Majority of the N-terminal domain (NTD, in blue) consists of a flexible, intrinsically disordered region (IDR) that binds both target RNA (black line) and cellular cofactors (yellow circle) to form specific ribonucleoprotein complexes. The highly structured C-terminal domain (CTD, in red) contains an alpha–helix-rich globular domain and forms a homodimer stabilized by intermolecular interactions between two monomers (red and green) and Zinc cations (Zn²⁺) binding and then by holding each other with an arm from the NTD of other monomer (Yuan et al.2018).