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4e4v
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(Difference between revisions)
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4e4v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e4v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4e4v RCSB], [http://www.ebi.ac.uk/pdbsum/4e4v PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4e4v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e4v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4e4v RCSB], [http://www.ebi.ac.uk/pdbsum/4e4v PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/IMA2_HUMAN IMA2_HUMAN]] Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. | ||
==See Also== | ==See Also== | ||
Revision as of 15:59, 25 December 2014
The crystal structure of the dimeric human importin alpha 1 at 2.5 angstrom resolution.
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