Solution structure and dynamics of the bioactive retroviral M domain from Rous sarcoma virus

James M. McDonnell; David Fushman; Sean M. Cahill; Wenjun Zhou; Amy Wolven; Carol B. Wilson; Timothy D. Nelle; Marilyn D. Resh; John Wills; David Cowburn

doi:10.1006/jmbi.1998.1788

Solution structure and dynamics of the bioactive retroviral M domain from Rous sarcoma virus

James M. McDonnell, David Fushman, Sean M. Cahill, Wenjun Zhou, Amy Wolven, Carol B. Wilson, Timothy D. Nelle, Marilyn D. Resh, John Wills, David Cowburn

Research output: Contribution to journal › Article › peer-review

45 Scopus citations

Abstract

A biologically active construct of the retroviral M domain from the avian Rous sarcoma virus is defined and its solution structure described. This M domain is fully active in budding and infectivity without myristylation. In spite of a sequence homology level that suggests no relationship among M domains and the family of matrix proteins in mammalian retroviruses, the conserved structural elements of a central core allow an M domain sequence motif to be described for all retroviruses. The surface of the M domain has a highly clustered positive patch comprised of sequentially distant residues. An analysis of the backbone dynamics, incorporating rotational anisotropy, is used to estimate the thermodynamics of proposed domain oligomerization.

Original language	English (US)
Pages (from-to)	921-928
Number of pages	8
Journal	Journal of Molecular Biology
Volume	279
Issue number	4
DOIs	https://doi.org/10.1006/jmbi.1998.1788
State	Published - Jun 19 1998
Externally published	Yes

Keywords

Heteronuclear NMR spectroscopy
Protein dynamics
RSV matrix protein
Sequence homology
Three-dimensional structure

ASJC Scopus subject areas

Molecular Biology
Biophysics
Structural Biology

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10.1006/jmbi.1998.1788

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title = "Solution structure and dynamics of the bioactive retroviral M domain from Rous sarcoma virus",

abstract = "A biologically active construct of the retroviral M domain from the avian Rous sarcoma virus is defined and its solution structure described. This M domain is fully active in budding and infectivity without myristylation. In spite of a sequence homology level that suggests no relationship among M domains and the family of matrix proteins in mammalian retroviruses, the conserved structural elements of a central core allow an M domain sequence motif to be described for all retroviruses. The surface of the M domain has a highly clustered positive patch comprised of sequentially distant residues. An analysis of the backbone dynamics, incorporating rotational anisotropy, is used to estimate the thermodynamics of proposed domain oligomerization.",

keywords = "Heteronuclear NMR spectroscopy, Protein dynamics, RSV matrix protein, Sequence homology, Three-dimensional structure",

author = "McDonnell, {James M.} and David Fushman and Cahill, {Sean M.} and Wenjun Zhou and Amy Wolven and Wilson, {Carol B.} and Nelle, {Timothy D.} and Resh, {Marilyn D.} and John Wills and David Cowburn",

note = "Funding Information: This work was supported by grants from NIH: GM-47021 to D.C., CA-4782 to J.W.W., and CA-72309 to M.D.R., and from ACS: FRA-427 to J.W.W. J.M.M. was supported by a Hitchings-Elion Fellowship from the Burroughs-Wellcome Fund. The contributions of Melissa DePetris to early aspects of this project are gratefully acknowledged. ",

year = "1998",

month = jun,

day = "19",

doi = "10.1006/jmbi.1998.1788",

language = "English (US)",

volume = "279",

pages = "921--928",

journal = "Journal of Molecular Biology",

issn = "0022-2836",

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number = "4",

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T1 - Solution structure and dynamics of the bioactive retroviral M domain from Rous sarcoma virus

AU - McDonnell, James M.

AU - Fushman, David

AU - Cahill, Sean M.

AU - Zhou, Wenjun

AU - Wolven, Amy

AU - Wilson, Carol B.

AU - Nelle, Timothy D.

AU - Resh, Marilyn D.

AU - Wills, John

AU - Cowburn, David

N1 - Funding Information: This work was supported by grants from NIH: GM-47021 to D.C., CA-4782 to J.W.W., and CA-72309 to M.D.R., and from ACS: FRA-427 to J.W.W. J.M.M. was supported by a Hitchings-Elion Fellowship from the Burroughs-Wellcome Fund. The contributions of Melissa DePetris to early aspects of this project are gratefully acknowledged.

PY - 1998/6/19

Y1 - 1998/6/19

N2 - A biologically active construct of the retroviral M domain from the avian Rous sarcoma virus is defined and its solution structure described. This M domain is fully active in budding and infectivity without myristylation. In spite of a sequence homology level that suggests no relationship among M domains and the family of matrix proteins in mammalian retroviruses, the conserved structural elements of a central core allow an M domain sequence motif to be described for all retroviruses. The surface of the M domain has a highly clustered positive patch comprised of sequentially distant residues. An analysis of the backbone dynamics, incorporating rotational anisotropy, is used to estimate the thermodynamics of proposed domain oligomerization.

AB - A biologically active construct of the retroviral M domain from the avian Rous sarcoma virus is defined and its solution structure described. This M domain is fully active in budding and infectivity without myristylation. In spite of a sequence homology level that suggests no relationship among M domains and the family of matrix proteins in mammalian retroviruses, the conserved structural elements of a central core allow an M domain sequence motif to be described for all retroviruses. The surface of the M domain has a highly clustered positive patch comprised of sequentially distant residues. An analysis of the backbone dynamics, incorporating rotational anisotropy, is used to estimate the thermodynamics of proposed domain oligomerization.

KW - Heteronuclear NMR spectroscopy

KW - Protein dynamics

KW - RSV matrix protein

KW - Sequence homology

KW - Three-dimensional structure

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JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

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Solution structure and dynamics of the bioactive retroviral M domain from Rous sarcoma virus

Abstract

Keywords

ASJC Scopus subject areas

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