Summary: Matrix protein (MA), p15
This is the Wikipedia entry entitled "Retroviral matrix protein". More...
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Retroviral matrix protein Edit Wikipedia article
Matrix proteins are produced as N-terminal domains of Gag precursor polyproteins. The Gag polyprotein directs the assembly and release of virus particles from infected cells. The Gag polyprotein has three domains required for activity: an N-terminal membrane-binding (M) domain (which corresponds to the matrix protein) that directs Gag to the plasma membrane, an interaction (I) domain involved in Gag aggregation, and a late assembly (L) domain that mediates the budding process . During viral maturation, the Gag polyprotein is cleaved by the retroviral protease into several corresponding structural proteins, yielding the matrix (MA), capsid (CA), and nucleocapsid (NC) proteins, and some smaller peptides. Gag-derived proteins govern the entire assembly and release of the virus particles, with matrix proteins playing key roles in Gag stability, capsid assembly, transport and budding.
structure of moloney murine leukaemia virus matrix protein
Although matrix proteins from different viruses appear to perform similar functions and can have similar structural folds, their primary sequences can be very different. Typical matrix proteins of retroviruses form an alpha helical bundle structure .
One family of these proteins represents matrix proteins from gammaretroviruses, such as Moloney murine leukemia virus (MoMLV), feline leukemia virus (FLV), and feline sarcoma virus (FESV). This family also includes matrix proteins from several eukaryotic endogenous retroviruses, which arise when one or more copies of the retroviral genome becomes integrated into the host genome.
m-domain from gag polyprotein of rous sarcoma virus, nmr, 20 structures
Another family represents the M domain of the Gag polyprotein found in avian retroviruses. It includes Gag polyproteins from several avian endogenous retroviruses.
solution structure of the m-pmv wild type matrix protein (p10)
Matrix proteins are also components of beta-retroviruses such as Mason-Pfizer monkey virus (MPMV) and mouse mammary tumor virus (MMTV) . This entry also identifies matrix proteins from several eukaryotic endogenous retroviruses.
crystal structure of equine infectious anaemia virus matrix antigen (eiav ma)
- Conte MR, Matthews S (July 1998). "Retroviral matrix proteins: a structural perspective". Virology 246 (2): 191–8. doi:10.1006/viro.1998.9206. PMID 9657938.
- Parent LJ, Cairns TM, Albert JA, Wilson CB, Wills JW, Craven RC (January 2000). "RNA dimerization defect in a Rous sarcoma virus matrix mutant". J. Virol. 74 (1): 164–72. doi:10.1128/jvi.74.1.164-172.2000. PMC 111525. PMID 10590103.
- McDonnell JM, Fushman D, Cahill SM, Zhou W, Wolven A, Wilson CB, Nelle TD, Resh MD, Wills J, Cowburn D (June 1998). "Solution structure and dynamics of the bioactive retroviral M domain from Rous sarcoma virus". J. Mol. Biol. 279 (4): 921–8. doi:10.1006/jmbi.1998.1788. PMID 9642071.
- Riffel N, Harlos K, Iourin O, Rao Z, Kingsman A, Stuart D, Fry E (December 2002). "Atomic resolution structure of Moloney murine leukemia virus matrix protein and its relationship to other retroviral matrix proteins". Structure 10 (12): 1627–36. doi:10.1016/S0969-2126(02)00896-1. PMID 12467570.
- Baker SJ, Cosenza SC, Reddy EP (September 1998). "The role of v-Fgr myristoylation and the Gag domain in membrane binding and cellular transformation". Virology 249 (1): 1–11. doi:10.1006/viro.1998.9323. PMID 9740771.
- Gifford R, Tristem M (May 2003). "The evolution, distribution and diversity of endogenous retroviruses". Virus Genes 26 (3): 291–315. doi:10.1023/A:1024455415443. PMID 12876457.
- Borisenko L (2003). "Avian endogenous retroviruses". Folia Biol. (Praha) 49 (5): 177–82. PMID 14680291.
- Stansell E, Tytler E, Walter MR, Hunter E (May 2004). "An early stage of Mason-Pfizer monkey virus budding is regulated by the hydrophobicity of the Gag matrix domain core". J. Virol. 78 (10): 5023–31. doi:10.1128/jvi.78.10.5023-5031.2004. PMC 400380. PMID 15113883.
- Poon DT, Li G, Aldovini A (March 1998). "Nucleocapsid and matrix protein contributions to selective human immunodeficiency virus type 1 genomic RNA packaging". J. Virol. 72 (3): 1983–93. PMC 109491. PMID 9499052.
Matrix protein (MA), p15 Provide feedback
The matrix protein, p15, is encoded by the gag gene. MA is involved in pathogenicity .
Pozsgay JM, Beilharz MW, Wines BD, Hess AD, Pitha PM; , J Virol 1993;67:5989-5999.: The MA (p15) and p12 regions of the gag gene are sufficient for the pathogenicity of the murine AIDS virus. PUBMED:7690416 EPMC:7690416
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR000840
Retroviral matrix proteins (or major core proteins) are components of envelope-associated capsids, which line the inner surface of virus envelopes and are associated with viral membranes [PUBMED:9657938]. Matrix proteins are produced as part of Gag precursor polyproteins. During viral maturation, the Gag polyprotein is cleaved into major structural proteins by the viral protease, yielding the matrix (MA), capsid (CA), nucleocapsid (NC), and some smaller peptides. Gag-derived proteins govern the entire assembly and release of the virus particles, with matrix proteins playing key roles in Gag stability, capsid assembly, transport and budding. Although matrix proteins from different retroviruses appear to perform similar functions and can have similar structural folds, their primary sequences can be very different.
This entry represents matrix proteins from gamma-retroviruses, such as Moloney murine leukemia virus (MoMLV), Feline leukemia virus (FLV), and Feline sarcoma virus (FESV) [PUBMED:12467570, PUBMED:9740771]. This entry also identifies matrix proteins from several eukaryotic endogenous retroviruses, which arise when one or more copies of the retroviral genome becomes integrated into the host genome [PUBMED:12876457].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Cellular component||viral capsid (GO:0019028)|
|Molecular function||structural molecule activity (GO:0005198)|
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|Seed source:||Pfam-B_229 (release 3.0)|
|Author:||Finn RD, Bateman A|
|Number in seed:||9|
|Number in full:||296|
|Average length of the domain:||123.90 aa|
|Average identity of full alignment:||61 %|
|Average coverage of the sequence by the domain:||20.54 %|
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build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||14|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Gag_MA domain has been found. There are 4 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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