1bm4

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[[Image:1bm4.gif|left|200px]]
 
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==MOMLV CAPSID PROTEIN MAJOR HOMOLOGY REGION PEPTIDE ANALOG==
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The line below this paragraph, containing "STRUCTURE_1bm4", creates the "Structure Box" on the page.
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<StructureSection load='1bm4' size='340' side='right'caption='[[1bm4]]' 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'>[[1bm4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Moloney_murine_leukemia_virus Moloney murine leukemia virus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BM4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BM4 FirstGlance]. <br>
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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</td></tr>
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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=1bm4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bm4 OCA], [https://pdbe.org/1bm4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bm4 RCSB], [https://www.ebi.ac.uk/pdbsum/1bm4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bm4 ProSAT]</span></td></tr>
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{{STRUCTURE_1bm4| PDB=1bm4 | SCENE= }}
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</table>
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== Function ==
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'''MOMLV CAPSID PROTEIN MAJOR HOMOLOGY REGION PEPTIDE ANALOG'''
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[https://www.uniprot.org/uniprot/GAG_MLVMS GAG_MLVMS] 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.<ref>PMID:19864377</ref> 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).<ref>PMID:19864377</ref> Capsid protein p30 forms the spherical core of the virion that encapsulates the genomic RNA-nucleocapsid complex (By similarity).<ref>PMID:19864377</ref> 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.<ref>PMID:19864377</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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==Overview==
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Check<jmol>
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The capsid domain of retroviral Gag proteins possesses a single highly conserved subdomain termed the major homology region (MHR). While the mutagenesis of residues in the MHR will impair virus infectivity, the precise solution structure and function of the MHR is not known. To aid the structure/function characterization of the MHR, the structures of synthetic peptides encompassing the MHR of the human immunodeficiency virus type I (HIV-1) and Moloney murine leukemia virus (MoMLV) capsid proteins were investigated by several techniques. Homology-based secondary-structure prediction suggested that the HIV-1 and MoMLV peptides could form 50% and 38% alpha-helix, respectively. CD studies indicated that, in the presence of 50% trifluoroethanol, the HIV-1 peptide adopts an alpha-helical structure over half of its length, while the MoMLV peptide is over one third alpha-helix. Further analysis by 1H-NMR suggested that the C-terminal portion of the MHR of each virus forms a helix in aqueous solution. Distance-geometry structures of each peptide were calculated from NOE distance restraints and were refined by restrained molecular dynamics. The C-terminal halves of both peptides were observed to be in an alpha-helical conformation, while the N-terminal halves were disordered. Furthermore, both helices were amphipathic with high conservation of amino acid side-chain character, suggesting that a conserved helical MHR C-terminus is essential to retroviral capsid protein function.
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bm/1bm4_consurf.spt"</scriptWhenChecked>
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==About this Structure==
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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1BM4 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BM4 OCA].
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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==Reference==
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1bm4 ConSurf].
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Solution structures of human immunodeficiency virus type 1 (HIV-1) and moloney murine leukemia virus (MoMLV) capsid protein major-homology-region peptide analogs by NMR spectroscopy., Clish CB, Peyton DH, Barklis E, Eur J Biochem. 1998 Oct 1;257(1):69-77. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9799104 9799104]
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<div style="clear:both"></div>
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[[Category: Single protein]]
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== References ==
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[[Category: Barklis, E.]]
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<references/>
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[[Category: Clish, C B.]]
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__TOC__
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[[Category: Peyton, D H.]]
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</StructureSection>
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[[Category: Capsid]]
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[[Category: Large Structures]]
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[[Category: Major homology region]]
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[[Category: Moloney murine leukemia virus]]
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[[Category: Mhr]]
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[[Category: Barklis E]]
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[[Category: Moloney murine leukemia virus capsid protein]]
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[[Category: Clish CB]]
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[[Category: Momlv]]
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[[Category: Peyton DH]]
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[[Category: Mu-mlv]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:41:15 2008''
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Current revision

MOMLV CAPSID PROTEIN MAJOR HOMOLOGY REGION PEPTIDE ANALOG

PDB ID 1bm4

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