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| | ==C-terminal zinc knuckle of the HIVNCp7== | | ==C-terminal zinc knuckle of the HIVNCp7== |
| - | <StructureSection load='2l44' size='340' side='right'caption='[[2l44]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2l44' size='340' side='right'caption='[[2l44]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2l44]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L44 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L44 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2l44]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L44 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L44 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2l45|2l45]], [[2l46|2l46]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=2l44 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l44 OCA], [https://pdbe.org/2l44 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l44 RCSB], [https://www.ebi.ac.uk/pdbsum/2l44 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l44 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=2l44 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l44 OCA], [https://pdbe.org/2l44 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l44 RCSB], [https://www.ebi.ac.uk/pdbsum/2l44 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l44 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/Q9YP46_9HIV1 Q9YP46_9HIV1]] Capsid protein p24 forms the conical core of the virus that encapsulates the genomic RNA-nucleocapsid complex (By similarity).[SAAS:SAAS012344_004_008806] Nucleocapsid protein p7 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers (By similarity).[SAAS:SAAS012344_004_011858]
| + | [https://www.uniprot.org/uniprot/Q9YP46_9HIV1 Q9YP46_9HIV1] Capsid protein p24 forms the conical core of the virus that encapsulates the genomic RNA-nucleocapsid complex (By similarity).[SAAS:SAAS012344_004_008806] Nucleocapsid protein p7 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers (By similarity).[SAAS:SAAS012344_004_011858] |
| | <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: Human immunodeficiency virus 1]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Cabrita, E J]] | + | [[Category: Cabrita EJ]] |
| - | [[Category: Erhardt, S]] | + | [[Category: Erhardt S]] |
| - | [[Category: Farrell, N P]] | + | [[Category: Farrell NP]] |
| - | [[Category: Quintal, S M.O]] | + | [[Category: Quintal SMO]] |
| - | [[Category: Viegas, A J.M]] | + | [[Category: Viegas AJM]] |
| - | [[Category: Hiv]]
| + | |
| - | [[Category: Metal binding protein]]
| + | |
| - | [[Category: Ncp7]]
| + | |
| - | [[Category: Platinum]]
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| Structural highlights
Function
Q9YP46_9HIV1 Capsid protein p24 forms the conical core of the virus that encapsulates the genomic RNA-nucleocapsid complex (By similarity).[SAAS:SAAS012344_004_008806] Nucleocapsid protein p7 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers (By similarity).[SAAS:SAAS012344_004_011858]
Publication Abstract from PubMed
This paper describes for the first time the intimate molecular details of the association between a platinated oligonucleotide and a zinc finger peptide. Site-specific platination of the guanine in a single-stranded hexanucleotide gave {[Pt(dien)d(5'-TACGCC-3')], Pt(dien)(6-mer)} (II) characterized by mass spectrometry and (1)H nuclear magnetic resonance (NMR) spectroscopy. The work extends the study of platinum-nucleobase complex-zinc finger interactions using small molecules such as [Pt(dien)(9-EtGua)](2+) (I). The structure of the (34-52) C-terminal finger of HIV nucleocapsid protein HIVNCp7 (ZF1) was characterized by (1)H NMR spectroscopy and compared with that of the N-terminal single finger and the two-finger "intact" NCp7. Interaction of II with ZF1 results in significant changes in comparison to the "free" uncomplexed hexanucleotide; the major changes occurring for Trp37 resonances that are broadened and moved upfield, and other major shifts are for Gln45 (Hepsilon21, Hgamma3, Qbeta), Met46 (NH, Hgamma2), Lys47 (NH, Qgamma), and Glu50 (Hgamma2, Hgamma3). The Zn-Cys/His chemical shifts show only marginal deviations. The solution structures of ZF1 and the 6-mer-ZF1 and II-ZF1 adducts were calculated from the nuclear Overhauser effect spectroscopy-derived distance constraints. The DNA position in the II-ZF1 adduct is completely different than in the absence of platinum. Major differences are the appearance of new Met46-Cyt6 H5 and Trp37-Cyt5 H5 contacts but severe weakening of the Trp37-Gua4 contact, attributed to the steric effects caused by Gua4 platination, accompanied by a change in the position of the aromatic ring. The results demonstrate the feasibility of targeting specific ZF motifs with DNA-tethered coordination compounds, such as Pt compounds and Co macrocycles, with implications for drug targetting and indeed the intimate mechanisms of DNA repair of platinated DNA.
Platinated DNA affects zinc finger conformation. Interaction of a platinated single-stranded oligonucleotide and the C-terminal zinc finger of nucleocapsid protein HIVNCp7.,Quintal S, Viegas A, Erhardt S, Cabrita EJ, Farrell NP Biochemistry. 2012 Feb 28;51(8):1752-61. Epub 2012 Feb 14. PMID:22303928[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Quintal S, Viegas A, Erhardt S, Cabrita EJ, Farrell NP. Platinated DNA affects zinc finger conformation. Interaction of a platinated single-stranded oligonucleotide and the C-terminal zinc finger of nucleocapsid protein HIVNCp7. Biochemistry. 2012 Feb 28;51(8):1752-61. Epub 2012 Feb 14. PMID:22303928 doi:10.1021/bi201834g
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