5b56: Difference between revisions
New page: '''Unreleased structure''' The entry 5b56 is ON HOLD Authors: Miyatake, H., Sanjoh, A., Matusda, G., Murakami, T., Murakami, H., Hagiwara, K., Yokoyama, M., Sato, H., Miyamoto, Y., Dohm... |
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The | ==Crystal structure of HIV-1 VPR C-Terminal domain and DIBB-M-Importin-Alpha2 complex== | ||
<StructureSection load='5b56' size='340' side='right'caption='[[5b56]], [[Resolution|resolution]] 2.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5b56]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/HIV-1_M:B_89.6 HIV-1 M:B_89.6] 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=5B56 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5B56 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]] 2.3Å</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=5b56 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b56 OCA], [https://pdbe.org/5b56 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5b56 RCSB], [https://www.ebi.ac.uk/pdbsum/5b56 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5b56 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. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Viral protein R (Vpr) is an accessory gene product of human immunodeficiency virus type 1 (HIV-1) that plays multiple important roles associated with viral replication. Structural studies using NMR have revealed that Vpr consists of three alpha-helices and contains flexible N- and C-termini. However, the molecular mechanisms associated with Vpr function have not been elucidated. To investigate Vpr multifunctionality, we performed an X-ray crystallographic study of Vpr complexes containing importin-alpha, a known Vpr binding partner present in host cells. Elucidation of the crystal structure revealed that the flexible C-terminus changes its conformation to a twisted beta-turn via an induced-fit mechanism, enabling binding to a minor nuclear localization signal (NLS) site of importin-alpha. The Vpr C-terminus can also bind with major NLS sites of importin-alpha in an extended conformation in different ways. These results, which represent the first reported crystallographic analysis of Vpr, demonstrate the multifunctional aspects that enable Vpr interaction with a variety of cellular proteins. | |||
Molecular Mechanism of HIV-1 Vpr for Binding to Importin-alpha.,Miyatake H, Sanjoh A, Murakami T, Murakami H, Matsuda G, Hagiwara K, Yokoyama M, Sato H, Miyamoto Y, Dohmae N, Aida Y J Mol Biol. 2016 May 12. pii: S0022-2836(16)30140-1. doi:, 10.1016/j.jmb.2016.05.003. PMID:27181198<ref>PMID:27181198</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5b56" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: | ==See Also== | ||
[[Category: | *[[Importin 3D structures|Importin 3D structures]] | ||
[[Category: Matusda | *[[Vpr protein|Vpr protein]] | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: Murakami | </StructureSection> | ||
[[Category: Sato | [[Category: HIV-1 M:B_89 6]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Mus musculus]] | |||
[[Category: Aida Y]] | |||
[[Category: Dohmae N]] | |||
[[Category: Hagiwara K]] | |||
[[Category: Matusda G]] | |||
[[Category: Miyamoto Y]] | |||
[[Category: Miyatake H]] | |||
[[Category: Murakami H]] | |||
[[Category: Murakami T]] | |||
[[Category: Sanjoh A]] | |||
[[Category: Sato H]] | |||
[[Category: Yokoyama M]] | |||
Latest revision as of 19:00, 8 November 2023
Crystal structure of HIV-1 VPR C-Terminal domain and DIBB-M-Importin-Alpha2 complexCrystal structure of HIV-1 VPR C-Terminal domain and DIBB-M-Importin-Alpha2 complex
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. Publication Abstract from PubMedViral protein R (Vpr) is an accessory gene product of human immunodeficiency virus type 1 (HIV-1) that plays multiple important roles associated with viral replication. Structural studies using NMR have revealed that Vpr consists of three alpha-helices and contains flexible N- and C-termini. However, the molecular mechanisms associated with Vpr function have not been elucidated. To investigate Vpr multifunctionality, we performed an X-ray crystallographic study of Vpr complexes containing importin-alpha, a known Vpr binding partner present in host cells. Elucidation of the crystal structure revealed that the flexible C-terminus changes its conformation to a twisted beta-turn via an induced-fit mechanism, enabling binding to a minor nuclear localization signal (NLS) site of importin-alpha. The Vpr C-terminus can also bind with major NLS sites of importin-alpha in an extended conformation in different ways. These results, which represent the first reported crystallographic analysis of Vpr, demonstrate the multifunctional aspects that enable Vpr interaction with a variety of cellular proteins. Molecular Mechanism of HIV-1 Vpr for Binding to Importin-alpha.,Miyatake H, Sanjoh A, Murakami T, Murakami H, Matsuda G, Hagiwara K, Yokoyama M, Sato H, Miyamoto Y, Dohmae N, Aida Y J Mol Biol. 2016 May 12. pii: S0022-2836(16)30140-1. doi:, 10.1016/j.jmb.2016.05.003. PMID:27181198[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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