4b8o: Difference between revisions
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<StructureSection load='4b8o' size='340' side='right'caption='[[4b8o]], [[Resolution|resolution]] 2.08Å' scene=''> | <StructureSection load='4b8o' size='340' side='right'caption='[[4b8o]], [[Resolution|resolution]] 2.08Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4b8o]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/ ] and [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[4b8o]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Macaca_mulatta_polyomavirus_1 Macaca mulatta polyomavirus 1] and [https://en.wikipedia.org/wiki/Oryza_sativa_Japonica_Group Oryza sativa Japonica Group]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B8O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4B8O FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.084Å</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=4b8o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b8o OCA], [https://pdbe.org/4b8o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4b8o RCSB], [https://www.ebi.ac.uk/pdbsum/4b8o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4b8o ProSAT]</span></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=4b8o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b8o OCA], [https://pdbe.org/4b8o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4b8o RCSB], [https://www.ebi.ac.uk/pdbsum/4b8o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4b8o ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/A7XWN5_SV40 A7XWN5_SV40] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Macaca mulatta polyomavirus 1]] | ||
[[Category: | [[Category: Oryza sativa Japonica Group]] | ||
[[Category: | [[Category: Boden M]] | ||
[[Category: | [[Category: Chang C-W]] | ||
[[Category: | [[Category: Counago RLM]] | ||
[[Category: | [[Category: Kobe B]] | ||
[[Category: | [[Category: Williams SJ]] | ||
Latest revision as of 13:58, 9 May 2024
rImp_alpha_SV40TAgNLSrImp_alpha_SV40TAgNLS
Structural highlights
FunctionPublication Abstract from PubMedIn the classical nucleocytoplasmic import pathway, nuclear localization signals (NLSs) in cargo proteins are recognized by the import receptor importin-alpha. Importin-alpha has two separate NLS binding sites (the major and the minor site), both of which recognize positively charged amino acid clusters in NLSs. Little is known about the molecular basis of the unique features of the classical nuclear import pathway in plants. We determined the crystal structure of rice (Oryza sativa) importin-alpha1a at 2-A resolution. The structure reveals that the autoinhibitory mechanism mediated by the importin-beta binding domain of importin-alpha operates in plants, with NLS-mimicking sequences binding to both minor and major NLS binding sites. Consistent with yeast and mammalian proteins, rice importin-alpha binds the prototypical NLS from simian virus 40 large T-antigen preferentially at the major NLS binding site. We show that two NLSs, previously described as plant specific, bind to and are functional with plant, mammalian, and yeast importin-alpha proteins but interact with rice importin-alpha more strongly. The crystal structures of their complexes with rice importin-alpha show that they bind to the minor NLS binding site. By contrast, the crystal structures of their complexes with mouse (Mus musculus) importin-alpha show preferential binding to the major NLS binding site. Our results reveal the molecular basis of a number of features of the classical nuclear transport pathway specific to plants. Crystal Structure of Rice Importin-alpha and Structural Basis of Its Interaction with Plant-Specific Nuclear Localization Signals.,Chang CW, Counago RL, Williams SJ, Boden M, Kobe B Plant Cell. 2012 Dec 18. PMID:23250448[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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