5wb5 | pdb_00005wb5

Leishmania IF4E-1 bound to Leishmania 4E-IP1

spinqualitylabelsall models 5wb5, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5wb5 is a 2 chain structure with sequence from Leishmania major. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.7Å Ligands: PEG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function E9ADE1_LEIMA Publication Abstract from PubMed Leishmania parasites are unicellular pathogens that are transmitted to humans through the bite of infected sandflies. Most of the regulation of their gene expression occurs post-transcriptionally, and the different patterns of gene expression required throughout the parasites' life cycle are regulated at the level of translation. Here, we report the X-ray crystal structure of the Leishmania cap-binding isoform 1, LeishIF4E-1, bound to a protein fragment of previously unknown function, Leish4E-IP1, that binds tightly to LeishIF4E-1. The molecular structure, coupled to NMR spectroscopy experiments and in vitro cap-binding assays, reveal that Leish4E-IP1 allosterically destabilizes the binding of LeishIF4E-1 to the 5' mRNA cap. We propose mechanisms through which Leish4E-IP1-mediated LeishIF4E-1 inhibition could regulate translation initiation in the human parasite. Structural basis for LeishIF4E-1 modulation by an interacting protein in the human parasite Leishmania major.,Meleppattu S, Arthanari H, Zinoviev A, Boeszoermenyi A, Wagner G, Shapira M, Leger-Abraham M Nucleic Acids Res. 2018 Mar 19. pii: 4942471. doi: 10.1093/nar/gky194. PMID:29562352 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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