This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1bax

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(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...)
Line 1: Line 1:
-
[[Image:1bax.gif|left|200px]]<br /><applet load="1bax" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1bax.gif|left|200px]]<br /><applet load="1bax" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1bax" />
caption="1bax" />
'''MASON-PFIZER MONKEY VIRUS MATRIX PROTEIN, NMR, AVERAGE STRUCTURE'''<br />
'''MASON-PFIZER MONKEY VIRUS MATRIX PROTEIN, NMR, AVERAGE STRUCTURE'''<br />
==Overview==
==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.
+
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==
-
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].
+
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==
Line 13: Line 13:
[[Category: Simian mason-pfizer virus]]
[[Category: Simian mason-pfizer virus]]
[[Category: Single protein]]
[[Category: Single protein]]
-
[[Category: Conte, M.R.]]
+
[[Category: Conte, M R.]]
[[Category: Hunter, E.]]
[[Category: Hunter, E.]]
[[Category: Klikova, M.]]
[[Category: Klikova, M.]]
Line 23: Line 23:
[[Category: polyprotein]]
[[Category: polyprotein]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:30:53 2007''
+
''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

Drag the structure with the mouse to rotate

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

Page seeded by OCA on Thu Feb 21 11:53:20 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools