4rxh

Crystal Structure of Importin-alpha from Neurospora crassa complexed with SV40NLS

spinqualitylabelsall models 4rxh, resolution 1.76Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4rxh is a 3 chain structure with sequence from Macaca mulatta polyomavirus 1 and Neurospora crassa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.7553Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9C2K9_NEUCS Publication Abstract from PubMed Neurospora crassa is a filamentous fungus that has been extensively studied as a model organism for eukaryotic biology, providing fundamental insights into cellular processes such as cell signaling, growth and differentiation. To advance in the study of this multicellular organism, an understanding of the specific mechanisms for protein transport into the cell nucleus is essential. Importin-alpha (Imp-alpha) is the receptor for cargo proteins that contain specific nuclear localization signals (NLSs) that play a key role in the classical nuclear import pathway. Structures of Imp-alpha from different organisms (yeast, rice, mouse, and human) have been determined, revealing that this receptor possesses a conserved structural scaffold. However, recent studies have demonstrated that the Impalpha mechanism of action may vary significantly for different organisms or for different isoforms from the same organism. Therefore, structural, functional, and biophysical characterization of different Impalpha proteins is necessary to understand the selectivity of nuclear transport. Here, we determined the first crystal structure of an Impalpha from a filamentous fungus which is also the highest resolution Impalpha structure already solved to date (1.75 A). In addition, we performed calorimetric analysis to determine the affinity and thermodynamic parameters of the interaction between Imp-alpha and the classical SV40 NLS peptide. The comparison of these data with previous studies on Impalpha proteins led us to demonstrate that N. crassa Imp-alpha possess specific features that are distinct from mammalian Imp-alpha but exhibit important similarities to rice Imp-alpha, particularly at the minor NLS binding site. Structure of Importin-alpha from a Filamentous Fungus in Complex with a Classical Nuclear Localization Signal.,Bernardes NE, Takeda AA, Dreyer TR, Freitas FZ, Bertolini MC, Fontes MR PLoS One. 2015 Jun 19;10(6):e0128687. doi: 10.1371/journal.pone.0128687., eCollection 2015. PMID:26091498 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Importin 3D structures Large T Antigen

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