6o5w | pdb_00006o5w

Crystal structure of MORC3 CW domain fused with viral influenza A NS1 peptide

spinqualitylabelsall models 6o5w, resolution 1.41Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6o5w is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.412Å Ligands: ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MORC3_HUMAN Publication Abstract from PubMed Microrchidia 3 (MORC3), a human ATPase linked to several autoimmune disorders, has been characterized both as a negative and positive regulator of influenza A virus. Here, we report that the CW domain of MORC3 (MORC3-CW) is targeted by the C-terminal tail of the influenza H3N2 protein NS1. The crystal structure of the MORC3-CW:NS1 complex shows that NS1 occupies the same binding site in CW that is normally occupied by histone H3, a physiological ligand of MORC3-CW. Comparable binding affinities of MORC3-CW to H3 and NS1 peptides and to the adjacent catalytic ATPase domain suggest that the viral protein can compete with the host histone for the association with CW, releasing MORC3 autoinhibition and activating the catalytic function of MORC3. Our structural, biochemical, and cellular analyses suggest that MORC3 might affect the infectivity of influenza virus and therefore has a role in cell immune response. MORC3 Is a Target of the Influenza A Viral Protein NS1.,Zhang Y, Ahn J, Green KJ, Vann KR, Black J, Brooke CB, Kutateladze TG Structure. 2019 Mar 29. pii: S0969-2126(19)30093-0. doi:, 10.1016/j.str.2019.03.015. PMID:31006586 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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