1bm4

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(Difference between revisions)

Revision as of 07:13, 22 September 2021

MOMLV CAPSID PROTEIN MAJOR HOMOLOGY REGION PEPTIDE ANALOG

Structural highlights

1bm4 is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1] 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).^[2] Capsid protein p30 forms the spherical core of the virion that encapsulates the genomic RNA-nucleocapsid complex (By similarity).^[3] 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.^[4]

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

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.

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:9799104^[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Jadwin JA, Rudd V, Sette P, Challa S, Bouamr F. Late domain-independent rescue of a release-deficient Moloney murine leukemia virus by the ubiquitin ligase itch. J Virol. 2010 Jan;84(2):704-15. doi: 10.1128/JVI.01319-09. Epub 2009 Oct 28. PMID:19864377 doi:http://dx.doi.org/10.1128/JVI.01319-09
↑ Jadwin JA, Rudd V, Sette P, Challa S, Bouamr F. Late domain-independent rescue of a release-deficient Moloney murine leukemia virus by the ubiquitin ligase itch. J Virol. 2010 Jan;84(2):704-15. doi: 10.1128/JVI.01319-09. Epub 2009 Oct 28. PMID:19864377 doi:http://dx.doi.org/10.1128/JVI.01319-09
↑ Jadwin JA, Rudd V, Sette P, Challa S, Bouamr F. Late domain-independent rescue of a release-deficient Moloney murine leukemia virus by the ubiquitin ligase itch. J Virol. 2010 Jan;84(2):704-15. doi: 10.1128/JVI.01319-09. Epub 2009 Oct 28. PMID:19864377 doi:http://dx.doi.org/10.1128/JVI.01319-09
↑ Jadwin JA, Rudd V, Sette P, Challa S, Bouamr F. Late domain-independent rescue of a release-deficient Moloney murine leukemia virus by the ubiquitin ligase itch. J Virol. 2010 Jan;84(2):704-15. doi: 10.1128/JVI.01319-09. Epub 2009 Oct 28. PMID:19864377 doi:http://dx.doi.org/10.1128/JVI.01319-09
↑ Clish CB, Peyton DH, Barklis E. 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. Eur J Biochem. 1998 Oct 1;257(1):69-77. PMID:9799104

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1bm4"

@@ Line 3: / Line 3: @@
 <StructureSection load='1bm4' size='340' side='right'caption='[[1bm4]], [[NMR_Ensembles_of_Models | 9 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1bm4]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BM4 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1bm4]] is a 1 chain structure. 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>
-</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=1bm4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bm4 OCA], [http://pdbe.org/1bm4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bm4 RCSB], [http://www.ebi.ac.uk/pdbsum/1bm4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1bm4 ProSAT]</span></td></tr>
+</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=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>
 </table>
 == Function ==
-[[http://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>
+[[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>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1bm4

From Proteopedia

Revision as of 07:13, 22 September 2021

MOMLV CAPSID PROTEIN MAJOR HOMOLOGY REGION PEPTIDE ANALOG

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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