Low resolution structural studies of Munc18c complexed with a Syntaxin-4/T4- Lysozyme Fusion

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dc.contributor.authorWhitten, AEen_AU
dc.contributor.authorRehman, AUen_AU
dc.contributor.authorHu, SHen_AU
dc.contributor.authorTnimov, Zen_AU
dc.contributor.authorChristie, MPen_AU
dc.contributor.authorKing, GJen_AU
dc.contributor.authorJarrott, RJen_AU
dc.contributor.authorNorwood, Sen_AU
dc.contributor.authorAlexandrov, Ken_AU
dc.contributor.authorCollins, BMen_AU
dc.contributor.authorMartin, JLen_AU
dc.date.accessioned2021-10-27T22:26:46Zen_AU
dc.date.available2021-10-27T22:26:46Zen_AU
dc.date.issued2016-11-29en_AU
dc.date.statistics2021-10-17en_AU
dc.description.abstractSoluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNARE) act at every intracellular trafficking pathway. Cognate v-SNAREs (e.g. VAMP) and t-SNAREs (Syntaxin (Sx) and SNAP) form a high affinity SNARE ternary complex (Sx-SNAP-VAMP) that brings the membranes together, triggering fusion. Syntaxins consist of a SNARE motif, and a three-helix bundle. In an open confirmation, the SNARE motif is free to form the SNARE ternary complex (stimulating fusion), but in the closed confirmation fusion is inhibited. Sec1p/Munc18 (SM) proteins bind to Sx, regulating SNARE mediated fusion [1], but their exact role is not well understood [2-4]. In the cell, Sx is bound to the membrane, and it is possible that this tethering may influence the manner in which it interacts with other proteins. As a means of investigating structural changes arising due to tethering, here, we investigate how the addition of a C-terminal T4-Lysozyme (soluble) fusion to Sx4 modulates its interaction with Munc18c. Preliminary low-resolution models of the Munc18c-Sx4T4 complex optimized against small-angle scattering data will be presented.en_AU
dc.identifier.citationWhitten, A. E., Rehman, A., Hu, S.-H., Tnimov, Z., Christie, M. P., King, G. J., Jarrott, R. J., Norwood, S., Alexandrov, K., Collins, B. M., & Martin, J. L. (2016). Low resolution structural studies of Munc18c complexed with a Syntaxin-4/T4- Lysozyme Fusion. Paper presented at 13th AINSE-ANBUG Neutron Scattering Symposium, Sydney, NSW, Australia, 29-30 November 2016.en_AU
dc.identifier.conferenceenddate30 November 2016en_AU
dc.identifier.conferencename13th AINSE-ANBUG Neutron Scattering Symposiumen_AU
dc.identifier.conferenceplaceSydney, NSW, Australiaen_AU
dc.identifier.conferencestartdate29 November 2016en_AU
dc.identifier.urihttps://apo.ansto.gov.au/dspace/handle/10238/12141en_AU
dc.language.isoenen_AU
dc.publisherAustralian Institute of Nuclear Science and Engineeringen_AU
dc.subjectProteinsen_AU
dc.subjectReceptorsen_AU
dc.subjectMembrane proteinsen_AU
dc.subjectSmall angle scatteringen_AU
dc.subjectResolutionen_AU
dc.subjectComplexesen_AU
dc.titleLow resolution structural studies of Munc18c complexed with a Syntaxin-4/T4- Lysozyme Fusionen_AU
dc.typeConference Abstracten_AU
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