3ZIP
minor-site specific NLS (A58)
Summary for 3ZIP
| Entry DOI | 10.2210/pdb3zip/pdb |
| Related | 3ZIN 3ZIO 3ZIQ 3ZIR |
| Descriptor | IMPORTIN SUBUNIT ALPHA-2, A58NLS (3 entities in total) |
| Functional Keywords | transport protein, nuclear import, nuclear localization signals |
| Biological source | MUS MUSCULUS (HOUSE MOUSE) More |
| Cellular location | Cytoplasm (By similarity): P52293 |
| Total number of polymer chains | 3 |
| Total formula weight | 52980.37 |
| Authors | Chang, C.-W.,Counago, R.M.,Williams, S.J.,Kobe, B. (deposition date: 2013-01-10, release date: 2013-08-21, Last modification date: 2023-12-20) |
| Primary citation | Chang, C.-W.,Counago, R.M.,Williams, S.J.,Boden, M.,Kobe, B. Distinctive Conformation of Minor Site-Specific Nuclear Localization Signals Bound to Importin-Alpha Traffic, 14:1144-, 2013 Cited by PubMed Abstract: Nuclear localization signals (NLSs) contain one or two clusters of basic residues and are recognized by the import receptor importin-α. There are two NLS-binding sites (major and minor) on importin-α and the major NLS-binding site is considered to be the primary binding site. Here, we used crystallographic and biochemical methods to investigate the binding between importin-α and predicted 'minor site-specific' NLSs: four peptide library-derived peptides, and the NLS from mouse RNA helicase II/Guα. The crystal structures reveal that these atypical NLSs indeed preferentially bind to the minor NLS-binding site. Unlike previously characterized NLSs, the C-terminal residues of these NLSs form an α-helical turn, stabilized by internal H-bond and cation-π interactions between the aromatic residues from the NLSs and the positively charged residues from importin-α. This helical turn sterically hinders binding at the major NLS-binding site, explaining the minor-site preference. Our data suggest the sequence RXXKR[K/X][F/Y/W]XXAF as the optimal minor NLS-binding site-specific motif, which may help identify novel proteins with atypical NLSs. PubMed: 23910026DOI: 10.1111/TRA.12098 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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