Calmodulin binds a highly extended HIV-1 MA protein that refolds upon its release

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dc.contributor.authorTaylor, JENen_AU
dc.contributor.authorChow, JYHen_AU
dc.contributor.authorJeffries, CMen_AU
dc.contributor.authorKwan, AHen_AU
dc.contributor.authorDuff, APen_AU
dc.contributor.authorHamilton, WAen_AU
dc.contributor.authorTrewhella, Jen_AU
dc.date.accessioned2014-03-07T01:40:22Zen_AU
dc.date.available2014-03-07T01:40:22Zen_AU
dc.date.issued2012-08-08en_AU
dc.date.statistics2014-03-07en_AU
dc.description.abstractCalmodulin (CaM) expression is upregulated upon HIV-1 infection and interacts with proteins involved in viral processing, including the multifunctional HIV-1 MA protein. We present here the results of studies utilizing small-angle neutron scattering with contrast variation that, when considered in the light of earlier fluorescence and NMR data, show CaM binds MA in an extended open-clamp conformation via interactions with two tryptophans that are widely spaced in sequence and space. The interaction requires a disruption of the MA tertiary fold such that MA becomes highly extended in a long snakelike conformation. The CaM-MA interface is extensive, covering ∼70% of the length of the MA such that regions known to be important in MA interactions with critical binding partners would be impacted. The CaM conformation is semiextended and as such is distinct from the classical CaM-collapse about short α-helical targets. NMR data show that upon dissociation of the CaM-MA complex, either by the removal of Ca2+ or increasing ionic strength, MA reforms its native tertiary contacts. Thus, we observe a high level of structural plasticity in MA that may facilitate regulation of its activities via intracellular Ca2+-signaling during viral processing. © 2012 Biophysical Society.en_AU
dc.identifier.citationTaylor, J. E. N, Chow, J. Y. H., Jeffries, C. M., Kwan, A. H., Duff, A. P., Hamilton, W. A., & Trewhella, J. (2012). Calmodulin binds a highly extended HIV-1 MA protein that refolds upon its release. Biophysical Journal, 103(3), 541-549. doi:10.1016/j.bpj.2012.06.042en_AU
dc.identifier.govdoc4622en_AU
dc.identifier.issn0006-3495en_AU
dc.identifier.issue3en_AU
dc.identifier.journaltitleBiophysical Journalen_AU
dc.identifier.pagination541-549en_AU
dc.identifier.urihttp://dx.doi.org/10.1016/j.bpj.2012.06.042en_AU
dc.identifier.urihttp://apo.ansto.gov.au/dspace/handle/10238/5246en_AU
dc.identifier.volume103en_AU
dc.language.isoenen_AU
dc.publisherCell Pressen_AU
dc.subjectAIDS virusen_AU
dc.subjectCalmodulinen_AU
dc.subjectPeptidesen_AU
dc.subjectProteinsen_AU
dc.subjectTryptophanen_AU
dc.subjectNMR imagingen_AU
dc.subjectViral diseasesen_AU
dc.titleCalmodulin binds a highly extended HIV-1 MA protein that refolds upon its releaseen_AU
dc.typeJournal Articleen_AU
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