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| | ==NMR structure of the HIV-2 nucleocapsid protein== | | ==NMR structure of the HIV-2 nucleocapsid protein== |
| - | <StructureSection load='2di2' size='340' side='right' caption='[[2di2]], [[NMR_Ensembles_of_Models | 13 NMR models]]' scene=''> | + | <StructureSection load='2di2' size='340' side='right'caption='[[2di2]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2di2]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DI2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2DI2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2di2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DI2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DI2 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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">[[1nc8|1nc8]]</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2di2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2di2 OCA], [http://pdbe.org/2di2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2di2 RCSB], [http://www.ebi.ac.uk/pdbsum/2di2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2di2 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=2di2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2di2 OCA], [https://pdbe.org/2di2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2di2 RCSB], [https://www.ebi.ac.uk/pdbsum/2di2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2di2 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GAG_HV2G1 GAG_HV2G1]] Matrix protein p17 targets Gag and Gag-pol polyproteins to the plasma membrane via a multipartite membrane binding signal. Also mediates nuclear localization of the preintegration complex (By similarity). Capsid protein p24 forms the conical core of the virus that encapsulates the genomic RNA-nucleocapsid complex (By similarity). Nucleocapsid protein p7 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers (By similarity). p6-gag plays a role in budding of the assembled particle by interacting with the host class E VPS proteins TSG101 and PDCD6IP/AIP1 (By similarity). | + | [https://www.uniprot.org/uniprot/GAG_HV2G1 GAG_HV2G1] Matrix protein p17 targets Gag and Gag-pol polyproteins to the plasma membrane via a multipartite membrane binding signal. Also mediates nuclear localization of the preintegration complex (By similarity). Capsid protein p24 forms the conical core of the virus that encapsulates the genomic RNA-nucleocapsid complex (By similarity). Nucleocapsid protein p7 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers (By similarity). p6-gag plays a role in budding of the assembled particle by interacting with the host class E VPS proteins TSG101 and PDCD6IP/AIP1 (By similarity). |
| | <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: Endoh, H]] | + | [[Category: Large Structures]] |
| - | [[Category: Kodera, Y]] | + | [[Category: Synthetic construct]] |
| - | [[Category: Kohno, T]] | + | [[Category: Endoh H]] |
| - | [[Category: Komatsu, H]] | + | [[Category: Kodera Y]] |
| - | [[Category: Maeda, T]] | + | [[Category: Kohno T]] |
| - | [[Category: Matsui, T]] | + | [[Category: Komatsu H]] |
| - | [[Category: Miyauchi, E]] | + | [[Category: Maeda T]] |
| - | [[Category: Sato, K]] | + | [[Category: Matsui T]] |
| - | [[Category: Tanaka, T]] | + | [[Category: Miyauchi E]] |
| - | [[Category: Hiv-2]]
| + | [[Category: Sato K]] |
| - | [[Category: Metal binding protein]]
| + | [[Category: Tanaka T]] |
| - | [[Category: Mutant]]
| + | |
| - | [[Category: Nucleocapsid protein]]
| + | |
| - | [[Category: Rna recognition]]
| + | |
| - | [[Category: Zinc finger]]
| + | |
| Structural highlights
Function
GAG_HV2G1 Matrix protein p17 targets Gag and Gag-pol polyproteins to the plasma membrane via a multipartite membrane binding signal. Also mediates nuclear localization of the preintegration complex (By similarity). Capsid protein p24 forms the conical core of the virus that encapsulates the genomic RNA-nucleocapsid complex (By similarity). Nucleocapsid protein p7 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers (By similarity). p6-gag plays a role in budding of the assembled particle by interacting with the host class E VPS proteins TSG101 and PDCD6IP/AIP1 (By similarity).
Publication Abstract from PubMed
NCp8 of HIV-2 contains two CCHC-type zinc fingers connected by a linker, and is involved in many critical steps of the virus life cycle. It was previously shown that the first zinc finger flanked by the linker is the minimal active domain for specific binding to viral RNA. In our previous study, we determined the three-dimensional structure of NCp8-f1, including the minimal active domain, and found that a hydrogen bond between Asn(11) N(delta)H and Arg(27) O stabilized the conformation of the linker in the vicinity of the zinc finger [Kodera et al. (1998) Biochemistry 37, 17704-17713]. In this study, RNA binding activities of NCp8-f1 and three types of its mutant peptides were analysed by native PAGE assay. The activity and three-dimensional structure of NCp8-f1/N11A, in which alanine is substituted for Asn(11) thereby affecting the conformation of the linker, was analyzed and compared with those of NCp8-f1. We demonstrated that the existence of Arg(4) and/or Lys(5) and Arg(26) and/or Arg(27) were necessary for binding RNA. Furthermore, the linker's flexible orientation, which is controlled by the hydrogen bond between Asn(11) N(delta)H and Arg(27) O, appears to be a structural basis for NCp8 existing as a multi-functional protein.
RNA recognition mechanism of the minimal active domain of the human immunodeficiency virus type-2 nucleocapsid protein.,Matsui T, Kodera Y, Endoh H, Miyauchi E, Komatsu H, Sato K, Tanaka T, Kohno T, Maeda T J Biochem. 2007 Feb;141(2):269-77. Epub 2007 Jan 3. PMID:17202191[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Matsui T, Kodera Y, Endoh H, Miyauchi E, Komatsu H, Sato K, Tanaka T, Kohno T, Maeda T. RNA recognition mechanism of the minimal active domain of the human immunodeficiency virus type-2 nucleocapsid protein. J Biochem. 2007 Feb;141(2):269-77. Epub 2007 Jan 3. PMID:17202191 doi:http://dx.doi.org/mvm037
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