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dc.contributor.authorChow, JYH-
dc.contributor.authorJeffries, CM-
dc.contributor.authorKwan, AH-
dc.contributor.authorGuss, JM-
dc.contributor.authorTrewhella, J-
dc.date.accessioned2010-09-01T04:45:42Z-
dc.date.available2010-09-01T04:45:42Z-
dc.date.issued2010-07-23-
dc.identifier.citationChow, J. Y. H., Jeffries, C. M., Kwan, A. H., Guss, J. M., & Trewhella, J. (2010). Calmodulin disrupts the structure of the HIV-1 MA protein. Journal of Molecular Biology, 400(4), 702-714. doi:10.1016/j.jmb.2010.05.022en_AU
dc.identifier.govdoc2563-
dc.identifier.issn0022-2836-
dc.identifier.urihttp://dx.doi.org/10.1016/j.jmb.2010.05.022en_AU
dc.identifier.urihttp://apo.ansto.gov.au/dspace/handle/10238/2401-
dc.description.abstractThe MA protein from HIV-1 is a small, multifunctional protein responsible for regulating various stages of the viral replication cycle. To achieve its diverse tasks, MA interacts with host cell proteins and it has been reported that one of these is the ubiquitous calcium-sensing calmodulin (CaM), which is up-regulated upon HIV-1 infection. The nature of the CaM–MA interaction has been the subject of structural studies, using peptides based on the MA sequence, that have led to conflicting conclusions. The results presented here show that CaM binds intact MA with 1:1 stoichiometry in a Ca2+-dependent manner and that the complex adopts a highly extended conformation in solution as revealed by small-angle X-ray scattering. Alterations in tryptophan fluorescence suggest that the two buried tryptophans (W16 and W36) located in the first two alpha-helices of MA mediate the CaM interaction. Major chemical shift changes occur in the NMR spectrum of MA upon complex formation, whereas chemical shift changes in the CaM spectrum are quite modest and are assigned to residues within the normal target protein-binding hydrophobic clefts of CaM. The NMR data indicate that CaM binds MA via its N- and C-terminal lobes and induces a dramatic conformational change involving a significant loss of secondary and tertiary structure within MA. Circular dichroism experiments suggest that MA loses ~ 20% of its α-helical content upon CaM binding. Thus, CaM binding is expected to impact upon the accessibility of interaction sites within MA that are involved in its various functions. © 2010, Elsevier Ltd.en_AU
dc.language.isoenen_AU
dc.publisherElsevieren_AU
dc.subjectSmall angle scatteringen_AU
dc.subjectAIDS virusen_AU
dc.subjectCalmodulinen_AU
dc.subjectChromatographyen_AU
dc.subjectProtein structureen_AU
dc.subjectTryptophanen_AU
dc.titleCalmodulin disrupts the structure of the HIV-1 MA proteinen_AU
dc.typeJournal Articleen_AU
dc.date.statistics2010-07-23-
Appears in Collections:Journal Articles

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