Atomic resolution structure of Moloney murine leukemia virus matrix protein and its relationship to other retroviral matrix proteins.

Matrix proteins associated with the viral membrane are important in the formation of the viral particle and in virus maturation. The 1.0 A crystal structure of the ecotropic Gammaretrovirus Moloney murine leukemia virus (M-MuLV) matrix protein reveals the conserved topology of other retroviral matri...

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Main Authors: Riffel, N, Harlos, K, Iourin, O, Rao, Z, Kingsman, A, Stuart, D, Fry, E
Format: Journal article
Language:English
Published: 2002
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author Riffel, N
Harlos, K
Iourin, O
Rao, Z
Kingsman, A
Stuart, D
Fry, E
author_facet Riffel, N
Harlos, K
Iourin, O
Rao, Z
Kingsman, A
Stuart, D
Fry, E
author_sort Riffel, N
collection OXFORD
description Matrix proteins associated with the viral membrane are important in the formation of the viral particle and in virus maturation. The 1.0 A crystal structure of the ecotropic Gammaretrovirus Moloney murine leukemia virus (M-MuLV) matrix protein reveals the conserved topology of other retroviral matrix proteins, despite undetectable sequence similarity. The N terminus (normally myristylated) is exposed and adjacent to a basic surface patch, features likely to contribute to membrane binding. The four proteins in the asymmetric unit make varied contacts. The M-MuLV matrix structure is intermediate, between those of the lentiviruses and other retroviruses. The protein fold appears to be maintained, in part, by the conservation of side chain packing, which may provide a useful tool for searching for weak distant similarities in proteins.
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spelling oxford-uuid:44274a2e-1df6-4c85-8134-cdbcfea622ab2022-03-26T14:59:52ZAtomic resolution structure of Moloney murine leukemia virus matrix protein and its relationship to other retroviral matrix proteins.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:44274a2e-1df6-4c85-8134-cdbcfea622abEnglishSymplectic Elements at Oxford2002Riffel, NHarlos, KIourin, ORao, ZKingsman, AStuart, DFry, EMatrix proteins associated with the viral membrane are important in the formation of the viral particle and in virus maturation. The 1.0 A crystal structure of the ecotropic Gammaretrovirus Moloney murine leukemia virus (M-MuLV) matrix protein reveals the conserved topology of other retroviral matrix proteins, despite undetectable sequence similarity. The N terminus (normally myristylated) is exposed and adjacent to a basic surface patch, features likely to contribute to membrane binding. The four proteins in the asymmetric unit make varied contacts. The M-MuLV matrix structure is intermediate, between those of the lentiviruses and other retroviruses. The protein fold appears to be maintained, in part, by the conservation of side chain packing, which may provide a useful tool for searching for weak distant similarities in proteins.
spellingShingle Riffel, N
Harlos, K
Iourin, O
Rao, Z
Kingsman, A
Stuart, D
Fry, E
Atomic resolution structure of Moloney murine leukemia virus matrix protein and its relationship to other retroviral matrix proteins.
title Atomic resolution structure of Moloney murine leukemia virus matrix protein and its relationship to other retroviral matrix proteins.
title_full Atomic resolution structure of Moloney murine leukemia virus matrix protein and its relationship to other retroviral matrix proteins.
title_fullStr Atomic resolution structure of Moloney murine leukemia virus matrix protein and its relationship to other retroviral matrix proteins.
title_full_unstemmed Atomic resolution structure of Moloney murine leukemia virus matrix protein and its relationship to other retroviral matrix proteins.
title_short Atomic resolution structure of Moloney murine leukemia virus matrix protein and its relationship to other retroviral matrix proteins.
title_sort atomic resolution structure of moloney murine leukemia virus matrix protein and its relationship to other retroviral matrix proteins
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