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| | <StructureSection load='1u7k' size='340' side='right'caption='[[1u7k]], [[Resolution|resolution]] 1.85Å' scene=''> | | <StructureSection load='1u7k' size='340' side='right'caption='[[1u7k]], [[Resolution|resolution]] 1.85Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1u7k]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Akr_(endogenous)_murine_leukemia_virus Akr (endogenous) murine leukemia virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U7K OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1U7K FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1u7k]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/AKR_(endogenous)_murine_leukemia_virus AKR (endogenous) murine leukemia virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U7K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1U7K FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GAG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11791 AKR (endogenous) murine leukemia virus])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1u7k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u7k OCA], [http://pdbe.org/1u7k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1u7k RCSB], [http://www.ebi.ac.uk/pdbsum/1u7k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1u7k 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=1u7k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u7k OCA], [https://pdbe.org/1u7k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1u7k RCSB], [https://www.ebi.ac.uk/pdbsum/1u7k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1u7k ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GAG_MLVAV GAG_MLVAV]] Gag polyprotein plays a role in budding and is processed by the viral protease during virion maturation outside the cell. During budding, it recruits, in a PPXY-dependent or independent manner, Nedd4-like ubiquitin ligases that conjugate ubiquitin molecules to Gag, or to Gag binding host factors. Interaction with HECT ubiquitin ligases probably link the viral protein to the host ESCRT pathway and facilitate release (By similarity). Matrix protein p15 targets Gag and gag-pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. Also mediates nuclear localization of the preintegration complex (By similarity). Nucleocapsid protein p10 is involved in the packaging and encapsidation of two copies of the genome. Binds with high affinity to conserved UCUG elements within the packaging signal, located near the 5'-end of the genome. This binding is dependent on genome dimerization (By similarity). | + | [https://www.uniprot.org/uniprot/GAG_MLVAV GAG_MLVAV] Gag polyprotein plays a role in budding and is processed by the viral protease during virion maturation outside the cell. During budding, it recruits, in a PPXY-dependent or independent manner, Nedd4-like ubiquitin ligases that conjugate ubiquitin molecules to Gag, or to Gag binding host factors. Interaction with HECT ubiquitin ligases probably link the viral protein to the host ESCRT pathway and facilitate release (By similarity). Matrix protein p15 targets Gag and gag-pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. Also mediates nuclear localization of the preintegration complex (By similarity). Nucleocapsid protein p10 is involved in the packaging and encapsidation of two copies of the genome. Binds with high affinity to conserved UCUG elements within the packaging signal, located near the 5'-end of the genome. This binding is dependent on genome dimerization (By similarity). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Haire, L F]] | + | [[Category: Haire LF]] |
| - | [[Category: Mortuza, G B]] | + | [[Category: Mortuza GB]] |
| - | [[Category: Smerdon, S J]] | + | [[Category: Smerdon SJ]] |
| - | [[Category: Stevens, A]] | + | [[Category: Stevens A]] |
| - | [[Category: Stoye, J P]] | + | [[Category: Stoye JP]] |
| - | [[Category: Taylor, I A]] | + | [[Category: Taylor IA]] |
| - | [[Category: Capsid]]
| + | |
| - | [[Category: Viral protein]]
| + | |
| Structural highlights
Function
GAG_MLVAV Gag polyprotein plays a role in budding and is processed by the viral protease during virion maturation outside the cell. During budding, it recruits, in a PPXY-dependent or independent manner, Nedd4-like ubiquitin ligases that conjugate ubiquitin molecules to Gag, or to Gag binding host factors. Interaction with HECT ubiquitin ligases probably link the viral protein to the host ESCRT pathway and facilitate release (By similarity). Matrix protein p15 targets Gag and gag-pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. Also mediates nuclear localization of the preintegration complex (By similarity). Nucleocapsid protein p10 is involved in the packaging and encapsidation of two copies of the genome. Binds with high affinity to conserved UCUG elements within the packaging signal, located near the 5'-end of the genome. This binding is dependent on genome dimerization (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Retroviruses are the aetiological agents of a range of human diseases including AIDS and T-cell leukaemias. They follow complex life cycles, which are still only partly understood at the molecular level. Maturation of newly formed retroviral particles is an essential step in production of infectious virions, and requires proteolytic cleavage of Gag polyproteins in the immature particle to form the matrix, capsid and nucleocapsid proteins present in the mature virion. Capsid proteins associate to form a dense viral core that may be spherical, cylindrical or conical depending on the genus of the virus. Nonetheless, these assemblies all appear to be composed of a lattice formed from hexagonal rings, each containing six capsid monomers. Here, we describe the X-ray structure of an individual hexagonal assembly from N-tropic murine leukaemia virus (N-MLV). The interface between capsid monomers is generally polar, consistent with weak interactions within the hexamer. Similar architectures are probably crucial for the regulation of capsid assembly and disassembly in all retroviruses. Together, these observations provide new insights into retroviral uncoating and how cellular restriction factors may interfere with viral replication.
High-resolution structure of a retroviral capsid hexameric amino-terminal domain.,Mortuza GB, Haire LF, Stevens A, Smerdon SJ, Stoye JP, Taylor IA Nature. 2004 Sep 23;431(7007):481-5. PMID:15386017[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Mortuza GB, Haire LF, Stevens A, Smerdon SJ, Stoye JP, Taylor IA. High-resolution structure of a retroviral capsid hexameric amino-terminal domain. Nature. 2004 Sep 23;431(7007):481-5. PMID:15386017 doi:10.1038/nature02915
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