1bax

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(New page: 200px<br /><applet load="1bax" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bax" /> '''MASON-PFIZER MONKEY VIRUS MATRIX PROTEIN, NM...)
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'''MASON-PFIZER MONKEY VIRUS MATRIX PROTEIN, NMR, AVERAGE STRUCTURE'''<br />
'''MASON-PFIZER MONKEY VIRUS MATRIX PROTEIN, NMR, AVERAGE STRUCTURE'''<br />
==Overview==
==Overview==
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The Mason-Pfizer monkey virus (M-PMV) is the prototype of the type D, retroviruses. In type B and D retroviruses, the Gag protein pre-assembles, before association with the membrane, whereas in type C retroviruses, (lentiviruses, BLV/HTLV group) Gag is targeted efficiently to the plasma, membrane, where the particle formation occurs. The N-terminal domain of, Gag, the matrix protein (MA), plays a critical role in determining this, morphogenic difference. We have determined the three-dimensional solution, structure of the M-PMV MA by heteronuclear nuclear magnetic resonance. The, protein contains four alpha-helices that are structurally similar to the, known type C MA structures. This similarity implies possible common, assembly units and membrane-binding mechanisms for type C and B/D, retroviruses. In addition to this, the interpretation of mutagenesis data, has enabled us to identify, for the first time, the structural basis of a, putative intracellular targeting motif.
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The Mason-Pfizer monkey virus (M-PMV) is the prototype of the type D retroviruses. In type B and D retroviruses, the Gag protein pre-assembles before association with the membrane, whereas in type C retroviruses (lentiviruses, BLV/HTLV group) Gag is targeted efficiently to the plasma membrane, where the particle formation occurs. The N-terminal domain of Gag, the matrix protein (MA), plays a critical role in determining this morphogenic difference. We have determined the three-dimensional solution structure of the M-PMV MA by heteronuclear nuclear magnetic resonance. The protein contains four alpha-helices that are structurally similar to the known type C MA structures. This similarity implies possible common assembly units and membrane-binding mechanisms for type C and B/D retroviruses. In addition to this, the interpretation of mutagenesis data has enabled us to identify, for the first time, the structural basis of a putative intracellular targeting motif.
==About this Structure==
==About this Structure==
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1BAX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Simian_mason-pfizer_virus Simian mason-pfizer virus]. This structure superseeds the now removed PDB entry 1AT7. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BAX OCA].
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1BAX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Simian_mason-pfizer_virus Simian mason-pfizer virus]. This structure supersedes the now removed PDB entry 1AT7. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BAX OCA].
==Reference==
==Reference==
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[[Category: Simian mason-pfizer virus]]
[[Category: Simian mason-pfizer virus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Conte, M.R.]]
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[[Category: Conte, M R.]]
[[Category: Hunter, E.]]
[[Category: Hunter, E.]]
[[Category: Klikova, M.]]
[[Category: Klikova, M.]]
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[[Category: polyprotein]]
[[Category: polyprotein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:30:53 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:53:20 2008''

Revision as of 09:53, 21 February 2008


1bax

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MASON-PFIZER MONKEY VIRUS MATRIX PROTEIN, NMR, AVERAGE STRUCTURE

Overview

The Mason-Pfizer monkey virus (M-PMV) is the prototype of the type D retroviruses. In type B and D retroviruses, the Gag protein pre-assembles before association with the membrane, whereas in type C retroviruses (lentiviruses, BLV/HTLV group) Gag is targeted efficiently to the plasma membrane, where the particle formation occurs. The N-terminal domain of Gag, the matrix protein (MA), plays a critical role in determining this morphogenic difference. We have determined the three-dimensional solution structure of the M-PMV MA by heteronuclear nuclear magnetic resonance. The protein contains four alpha-helices that are structurally similar to the known type C MA structures. This similarity implies possible common assembly units and membrane-binding mechanisms for type C and B/D retroviruses. In addition to this, the interpretation of mutagenesis data has enabled us to identify, for the first time, the structural basis of a putative intracellular targeting motif.

About this Structure

1BAX is a Single protein structure of sequence from Simian mason-pfizer virus. This structure supersedes the now removed PDB entry 1AT7. Full crystallographic information is available from OCA.

Reference

The three-dimensional solution structure of the matrix protein from the type D retrovirus, the Mason-Pfizer monkey virus, and implications for the morphology of retroviral assembly., Conte MR, Klikova M, Hunter E, Ruml T, Matthews S, EMBO J. 1997 Oct 1;16(19):5819-26. PMID:9312040

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