1bax
From Proteopedia
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
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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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