6bwa: Difference between revisions
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==Hendra virus W protein C-terminus in complex with Importin alpha 3 crystal form 2== | |||
<StructureSection load='6bwa' size='340' side='right' caption='[[6bwa]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6bwa]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BWA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BWA FirstGlance]. <br> | |||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6bvz|6bvz]], [[6bvv|6bvv]], [[6bvt|6bvt]], [[6bw0|6bw0]], [[6bw1|6bw1]], [[6bw9|6bw9]]</td></tr> | |||
[[Category: | <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=6bwa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bwa OCA], [http://pdbe.org/6bwa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bwa RCSB], [http://www.ebi.ac.uk/pdbsum/6bwa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bwa ProSAT]</span></td></tr> | ||
[[Category: Basler, C | </table> | ||
[[Category: Edwards, M | == Function == | ||
[[Category: Forwood, J | [[http://www.uniprot.org/uniprot/IMA3_HUMAN IMA3_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. In vitro, mediates the nuclear import of human cytomegalovirus UL84 by recognizing a non-classical NLS. In vitro, mediates the nuclear import of human cytomegalovirus UL84 by recognizing a non-classical NLS. | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Aragao, D]] | |||
[[Category: Basler, C F]] | |||
[[Category: Cross, E M]] | |||
[[Category: Edwards, M R]] | |||
[[Category: Forwood, J K]] | |||
[[Category: Smith, K M]] | |||
[[Category: Tsimbalyuk, S]] | [[Category: Tsimbalyuk, S]] | ||
[[Category: | [[Category: Complex]] | ||
[[Category: | [[Category: Hendra virus]] | ||
[[Category: | [[Category: Importin]] | ||
[[Category: Karyopherin]] | |||
[[Category: Phosphoprotein]] | |||
[[Category: Transport protein]] | |||
Revision as of 10:12, 4 July 2018
Hendra virus W protein C-terminus in complex with Importin alpha 3 crystal form 2Hendra virus W protein C-terminus in complex with Importin alpha 3 crystal form 2
Structural highlights
Function[IMA3_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. In vitro, mediates the nuclear import of human cytomegalovirus UL84 by recognizing a non-classical NLS. In vitro, mediates the nuclear import of human cytomegalovirus UL84 by recognizing a non-classical NLS. |
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