1kzs

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{{Seed}}
 
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[[Image:1kzs.png|left|200px]]
 
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==Structure of Human Immunodeficiency Virus Type 1 Vpr(34-51) Peptide in Aqueous TFE Solution==
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The line below this paragraph, containing "STRUCTURE_1kzs", creates the "Structure Box" on the page.
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<StructureSection load='1kzs' size='340' side='right'caption='[[1kzs]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1kzs]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_immunodeficiency_virus_type_1_(NEW_YORK-5_ISOLATE) Human immunodeficiency virus type 1 (NEW YORK-5 ISOLATE)]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KZS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KZS FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
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{{STRUCTURE_1kzs| PDB=1kzs | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1kzs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kzs OCA], [https://pdbe.org/1kzs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kzs RCSB], [https://www.ebi.ac.uk/pdbsum/1kzs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kzs ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/VPR_HV1N5 VPR_HV1N5] Involved in the transport of the viral pre-integration (PIC) complex to the nucleus during the early stages of the infection. This function is crucial for viral infection of non-dividing macrophages. May interact with karyopherin alpha/KPNA1 and KPNA2 to increase their affinity for proteins containing basic-type nuclear localization signal, including the viral matrix protein MA, thus facilitating the translocation of the viral genome into the nucleus. May also act directly at the nuclear pore complex, by binding nucleoporins phenylalanine-glycine (FG)-repeat regions (By similarity). May target specific host proteins for degradation by the 26S proteasome. Acts by associating with the cellular CUL4A-DDB1 E3 ligase complex through direct interaction with host VPRPB/DCAF-1. This change in the E3 ligase substrate specificity would result in cell cycle arrest or apoptosis in infected cells. Prevents infected cells from undergoing mitosis and proliferating, by inducing arrest or delay in the G2 phase of the cell cycle. This arrest creates a favorable environment for maximizing viral expression and production by rendering the HIV-1 LTR transcriptionally more active. In this context, Vpr stimulates gene expression driven by the HIV-1 LTR by interacting with human SP1, TFIIB and TFIID. Cell cycle arrest reportedly occurs within hours of infection and is not blocked by antiviral agents, suggesting that it is initiated by the Vpr carried into the virion. Additionally, Vpr induces apoptosis in a cell cycle dependent manner suggesting that these two effects are mechanistically linked. Interacts with mitochondrial permeability transition pore complex (PTPC). This interaction induces a rapid dissipation of the mitochondrial transmembrane potential, and mitochondrial release of apoptogenic proteins such as cytochrome C or apoptosis inducing factors. Detected in the serum and cerebrospinal fluid of AIDS patient, Vpr may also induce cell death to bystander cells (By similarity).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Human immunodeficiency virus type 1 protein R (HIV-1 Vpr) promotes nuclear entry of viral nucleic acids in nondividing cells, causes G(2) cell cycle arrest and is involved in cellular differentiation and cell death. Vpr subcellular localization is as variable as its functions. It is known, that consistent with its role in nuclear transport, Vpr localizes to the nuclear envelope of human cells. Further, a reported ion channel activity of Vpr is clearly dependent on its localization in or at membranes. We focused our structural studies on the secondary structure of a peptide consisting of residues 34-51 of HIV-1 Vpr. This part of Vpr plays an important role in Vpr oligomerization, contributes to cell cycle arrest activity, and is essential for virion incorporation and binding to HHR23A, a protein involved in DNA repair. Employing NMR spectroscopy we found this part of Vpr to be almost completely alpha helical in the presence of micelles, as well as in trifluoroethanol containing and methanol/chloroform solvent. Our results provide structural data suggesting residues 34-51 of Vpr to contain an amphipathic, leucine-zipper-like alpha helix, which serves as a basis for oligomerization of Vpr and its interactions with cellular and viral factors involved in subcellular localization and virion incorporation of Vpr.
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===Structure of Human Immunodeficiency Virus Type 1 Vpr(34-51) Peptide in Aqueous TFE Solution===
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Structure of human immunodeficiency virus type 1 Vpr(34-51) peptide in micelle containing aqueous solution.,Engler A, Stangler T, Willbold D Eur J Biochem. 2002 Jul;269(13):3264-9. PMID:12084067<ref>PMID:12084067</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1kzs" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_12084067}}, adds the Publication Abstract to the page
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*[[Vpr protein|Vpr protein]]
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(as it appears on PubMed at http://www.pubmed.gov), where 12084067 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_12084067}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1KZS is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KZS OCA].
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[[Category: Engler A]]
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[[Category: Stangler T]]
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==Reference==
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[[Category: Willbold D]]
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Structure of human immunodeficiency virus type 1 Vpr(34-51) peptide in micelle containing aqueous solution., Engler A, Stangler T, Willbold D, Eur J Biochem. 2002 Jul;269(13):3264-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12084067 12084067]
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[[Category: Single protein]]
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[[Category: Engler, A.]]
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[[Category: Stangler, T.]]
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[[Category: Willbold, D.]]
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[[Category: Hiv-1]]
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[[Category: Nmr]]
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[[Category: Peptide]]
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[[Category: Solution structure]]
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[[Category: Tfe]]
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[[Category: Vpr]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 11:23:00 2008''
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Current revision

Structure of Human Immunodeficiency Virus Type 1 Vpr(34-51) Peptide in Aqueous TFE Solution

PDB ID 1kzs

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