9l2w

Crystal structure of the C-terminal of viral responsive protein 15 (PmVRP15) from black tiger shrimp Penaeus monodon

spinqualitylabelsall models 9l2w, resolution 1.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9l2w is a 3 chain structure with sequence from Penaeus monodon. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.5Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function X2FU51_PENMO Publication Abstract from PubMed White spot syndrome virus (WSSV) is a major serious threat to black tiger shrimp farming. WSSV infection induces a host protein, viral responsive protein 15 (VRP15), for viral assembly and nuclear egress. Here, we showed that the C-terminal tail of VRP15 (VRP15-C) interacts directly with the viral nucleocapsid tegument protein WSV399. The crystal structure of VRP15-C was determined at 1.5 A. The structure showed that VRP15-C forms a dimer by forming an alpha-helix bundle structure and that the dimer further interacts with adjacent dimers to form a tetramer and a higher oligomer by intermolecular helix-helix interactions. The ability to form oligomeric forms may contribute to assembly of viral proteins to form a nucleocapsid of WSSV. Structure of the C-terminal of Viral Responsive Protein 15 (VRP15): A Key Protein During White Spot Syndrome Virus (WSSV) Infection.,Laohawutthichai P, Kim SY, Chek MF, Jatuyosporn T, Tassanakajon A, Krusong K, Hakoshima T J Mol Biol. 2025 Oct 1;437(19):169329. doi: 10.1016/j.jmb.2025.169329. Epub 2025 , Jul 8. PMID:40639753 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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