5uws | pdb_00005uws

Crystal Structure of X11L2 NES Peptide in complex with CRM1-Ran-RanBP1

spinqualitylabelsall models 5uws, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5uws is a 4 chain structure with sequence from Atcc 18824 and Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GNP, GOL, MG Related: 5uwi, 5uwh, 5uwj, 5uwu, 5uwo, 5uwp, 5uwq, 5uwr, 5uwt, 5uww Gene: RAN, ARA24, OK/SW-cl.81 (HUMAN), YRB1, CST20, HTN1, SFO1, YDR002W, YD8119.08 (ATCC 18824), CRM1, KAP124, XPO1, YGR218W, G8514 (ATCC 18824), X11L2 (HUMAN) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [RAN_HUMAN] GTP-binding protein involved in nucleocytoplasmic transport. Required for the import of protein into the nucleus and also for RNA export. Involved in chromatin condensation and control of cell cycle (By similarity). The complex with BIRC5/ survivin plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules. Acts as a negative regulator of the kinase activity of VRK1 and VRK2. Enhances AR-mediated transactivation. Transactivation decreases as the poly-Gln length within AR increases. [XPO1_YEAST] Receptor for the leucine-rich nuclear export signal (NES). [YRB1_YEAST] Important for the export of protein containing nuclear export signal (NES) out of the nucleus. Stimulates the GTPase activity of GSP1 and GSP2. Publication Abstract from PubMed Nuclear export receptor CRM1 binds highly variable nuclear export signals (NESs) in hundreds of different cargoes. Previously we have shown that CRM1 binds NESs in both polypeptide orientations (Fung et al., 2015). Here, we show crystal structures of CRM1 bound to eight additional NESs which reveal diverse conformations that range from loop-like to all-helix, which occupy different extents of the invariant NES-binding groove. Analysis of all NES structures show 5-6 distinct backbone conformations where the only conserved secondary structural element is one turn of helix that binds the central portion of the CRM1 groove. All NESs also participate in main chain hydrogen bonding with human CRM1 Lys568 side chain, which acts as a specificity filter that prevents binding of non-NES peptides. The large conformational range of NES backbones explains the lack of a fixed pattern for its 3-5 hydrophobic anchor residues, which in turn explains the large array of peptide sequences that can function as NESs. Nuclear export receptor CRM1 recognizes diverse conformations in nuclear export signals.,Fung HY, Fu SC, Chook YM Elife. 2017 Mar 10;6. pii: e23961. doi: 10.7554/eLife.23961. PMID:28282025 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Exportin GTP-binding protein

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