1u5o | pdb_00001u5o

Structure of the D23A mutant of the nuclear transport carrier NTF2

spinqualitylabelsall models 1u5o, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1u5o is a 2 chain structure with sequence from Buffalo rat. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1oun, 1ar0, 1ask Gene: Nutf2, Ntf2 (Buffalo rat) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [NTF2_RAT] Facilitates protein transport into the nucleus. Interacts with the nucleoporin p62 and with Ran. Acts at a relatively late stage of nuclear protein import, subsequent to the initial docking of nuclear import ligand at the nuclear envelope. Could be part of a multicomponent system of cytosolic factors that assemble at the pore complex during nuclear import (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Nuclear transport carriers interact with proteins of the nuclear pore complex (NPC) to transport their cargo across the nuclear envelope. One such carrier is nuclear transport factor 2 (NTF2), whose import cargo is the small GTPase Ran. A domain highly homologous to the small NTF2 protein (14kDa) is also found in a number of additional proteins, which together make up the NTF2 domain containing superfamily of proteins. Using structural, computational and biochemical analysis we have identified a functional site that is present throughout this superfamily, and our results indicate that this site functions as an NPC binding site in NTF2. Previously we showed that a D23A mutant of NTF2 exhibits increased affinity for the NPC. The mechanism of this mutation, however, was unknown as this region of NTF2 had not been implicated in binding to NPC proteins. Here we show that the D23A mutation in NTF2 does not result in gross structural changes affecting other known NPC binding sites. Instead, the D23 residue is located in an evolutionarily important region in the NTF2 domain containing superfamily, that in NTF2, is involved in binding to the NPC. Computational and biochemical identification of a nuclear pore complex binding site on the nuclear transport carrier NTF2.,Cushman I, Bowman BR, Sowa ME, Lichtarge O, Quiocho FA, Moore MS J Mol Biol. 2004 Nov 19;344(2):303-10. PMID:15522285 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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