X-ray and neutron reflectivity study of the membrane-bound CLIC1 protein at the air-water interface
dc.contributor.author | Hossain, KR | en_AU |
dc.contributor.author | Holt, SA | en_AU |
dc.contributor.author | Khamici, HA | en_AU |
dc.contributor.author | Valenzuela, SM | en_AU |
dc.date.accessioned | 2021-10-26T22:23:38Z | en_AU |
dc.date.available | 2021-10-26T22:23:38Z | en_AU |
dc.date.issued | 2016-11-29 | en_AU |
dc.date.statistics | 2021-10-12 | en_AU |
dc.description.abstract | The CLIC proteins are a ubiquitous family of Chloride Intracellular Ion Channel proteins that are evolutionarily conserved across species and exist as a soluble form and an integral membrane-bound form 1. The X-ray structure of the soluble form of a number of CLIC proteins has been solved and their putative transmembrane domain identified 2-5. However, the factors which facilitate the membrane insertion, the structural transition between these two forms and the structural features of the membrane-bound form for this class of proteins remain largely unknown. In an attempt to answer these questions, we have employed biophysical techniques to study the interaction of wild-type and mutant versions of the protein CLIC1 with monolayers prepared using various mixtures of different phospholipids and sterol molecules. Our findings have demonstrated that cholesterol plays a crucial role for the penetration of CLIC1 into the hydrophobic tails of the lipid monolayer with the protein occupying an area per molecule between 5-7 nm2. We have also demonstrated for the first time that CLIC1 interaction with cholesterol is dependent on the intact 3β-OH group in the sterol ring and that the GXXXG motif in CLIC1 acts as the cholesterol-binding site used by the protein for its initial recognition and binding to membrane cholesterol. | en_AU |
dc.identifier.citation | Hossain, K. R., Holt, S. A., Khamici, H. A., & Valenzuela, S. M. (2016). X-ray and neutron reflectivity study of the membrane-bound CLIC1 protein at the air-water interface. Paper presented at 13th AINSE-ANBUG Neutron Scattering Symposium, Sydney, NSW, Australia, 29-30 November 2016. | en_AU |
dc.identifier.conferenceenddate | 30 November 2016 | en_AU |
dc.identifier.conferencename | 13th AINSE-ANBUG Neutron Scattering Symposium | en_AU |
dc.identifier.conferenceplace | Sydney, NSW, Australia | en_AU |
dc.identifier.conferencestartdate | 29 November 2016 | en_AU |
dc.identifier.uri | https://apo.ansto.gov.au/dspace/handle/10238/12107 | en_AU |
dc.language.iso | en | en_AU |
dc.publisher | Australian Institute of Nuclear Science and Engineering | en_AU |
dc.subject | Proteins | en_AU |
dc.subject | Chlorides | en_AU |
dc.subject | Biophysics | en_AU |
dc.subject | Cholesterol | en_AU |
dc.subject | Phospholipids | en_AU |
dc.subject | Sterols | en_AU |
dc.title | X-ray and neutron reflectivity study of the membrane-bound CLIC1 protein at the air-water interface | en_AU |
dc.type | Conference Abstract | en_AU |