The p12 domain is unstructured in a murine leukemia virus p12-CA(N) Gag construct.

The Gag polyproteins of gammaretroviruses contain a conserved p12 domain between MA and CA that plays critical roles in virus assembly, reverse transcription and nuclear integration. Here we show using nuclear magnetic resonance, that p12 is unstructured in a Moloney murine leukemia virus (MMLV) Gag...

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Autores principales:	Sampson K Kyere, Prem Raj B Joseph, Michael F Summers
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2008
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/f66884fb6f2c425686b226c6b819755b
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spelling	oai:doaj.org-article:f66884fb6f2c425686b226c6b819755b2021-11-25T06:12:54ZThe p12 domain is unstructured in a murine leukemia virus p12-CA(N) Gag construct.1932-620310.1371/journal.pone.0001902https://doaj.org/article/f66884fb6f2c425686b226c6b819755b2008-04-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/18382677/?tool=EBIhttps://doaj.org/toc/1932-6203The Gag polyproteins of gammaretroviruses contain a conserved p12 domain between MA and CA that plays critical roles in virus assembly, reverse transcription and nuclear integration. Here we show using nuclear magnetic resonance, that p12 is unstructured in a Moloney murine leukemia virus (MMLV) Gag fragment that includes the N-terminal domain of CA (p12-CA(N)). Furthermore, no long range interactions were observed between the domains, as has been previously predicted. Flexibility appears to be a common feature of Gag "late" domains required for virus release during budding. Residues near the N-terminus of CA(N) that form a beta-hairpin in the mature CA protein are unfolded in p12-CA(N), consistent with proposals that hairpin formation helps trigger capsid assembly.Sampson K KyerePrem Raj B JosephMichael F SummersPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 3, Iss 4, p e1902 (2008)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Sampson K Kyere Prem Raj B Joseph Michael F Summers The p12 domain is unstructured in a murine leukemia virus p12-CA(N) Gag construct.
description	The Gag polyproteins of gammaretroviruses contain a conserved p12 domain between MA and CA that plays critical roles in virus assembly, reverse transcription and nuclear integration. Here we show using nuclear magnetic resonance, that p12 is unstructured in a Moloney murine leukemia virus (MMLV) Gag fragment that includes the N-terminal domain of CA (p12-CA(N)). Furthermore, no long range interactions were observed between the domains, as has been previously predicted. Flexibility appears to be a common feature of Gag "late" domains required for virus release during budding. Residues near the N-terminus of CA(N) that form a beta-hairpin in the mature CA protein are unfolded in p12-CA(N), consistent with proposals that hairpin formation helps trigger capsid assembly.
format	article
author	Sampson K Kyere Prem Raj B Joseph Michael F Summers
author_facet	Sampson K Kyere Prem Raj B Joseph Michael F Summers
author_sort	Sampson K Kyere
title	The p12 domain is unstructured in a murine leukemia virus p12-CA(N) Gag construct.
title_short	The p12 domain is unstructured in a murine leukemia virus p12-CA(N) Gag construct.
title_full	The p12 domain is unstructured in a murine leukemia virus p12-CA(N) Gag construct.
title_fullStr	The p12 domain is unstructured in a murine leukemia virus p12-CA(N) Gag construct.
title_full_unstemmed	The p12 domain is unstructured in a murine leukemia virus p12-CA(N) Gag construct.
title_sort	p12 domain is unstructured in a murine leukemia virus p12-ca(n) gag construct.
publisher	Public Library of Science (PLoS)
publishDate	2008
url	https://doaj.org/article/f66884fb6f2c425686b226c6b819755b
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_version_	1718414080703725568

The p12 domain is unstructured in a murine leukemia virus p12-CA(N) Gag construct.

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