8fk3: Difference between revisions
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The | ==Adeno-Associated Virus Porcine Origin capsid protein basic regions in complex with Importin-alpha 2== | ||
<StructureSection load='8fk3' size='340' side='right'caption='[[8fk3]], [[Resolution|resolution]] 2.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8fk3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Adeno-associated_virus_-_Po1 Adeno-associated virus - Po1] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8FK3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8FK3 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8fk3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8fk3 OCA], [https://pdbe.org/8fk3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8fk3 RCSB], [https://www.ebi.ac.uk/pdbsum/8fk3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8fk3 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/IMA1_MOUSE IMA1_MOUSE] 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== | |||
*[[Importin 3D structures|Importin 3D structures]] | |||
__TOC__ | |||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Adeno-associated virus - Po1]] | ||
[[Category: Forwood | [[Category: Large Structures]] | ||
[[Category: Hoad | [[Category: Mus musculus]] | ||
[[Category: Forwood KJ]] | |||
[[Category: Hoad M]] | |||
[[Category: Roby AJ]] | |||
Latest revision as of 13:08, 27 September 2023
Adeno-Associated Virus Porcine Origin capsid protein basic regions in complex with Importin-alpha 2Adeno-Associated Virus Porcine Origin capsid protein basic regions in complex with Importin-alpha 2
Structural highlights
FunctionIMA1_MOUSE 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 |
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