Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.bbapap.2007.12.005
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dc.titleTrimeric reassembly of the globular domain of human C1q
dc.contributor.authorTacnet, P.
dc.contributor.authorCheong, E.C.C.
dc.contributor.authorGoeltz, P.
dc.contributor.authorGhebrehiwet, B.
dc.contributor.authorArlaud, G.J.
dc.contributor.authorLiu, X.-Y.
dc.contributor.authorLesieur, C.
dc.date.accessioned2014-10-16T09:47:19Z
dc.date.available2014-10-16T09:47:19Z
dc.date.issued2008-03
dc.identifier.citationTacnet, P., Cheong, E.C.C., Goeltz, P., Ghebrehiwet, B., Arlaud, G.J., Liu, X.-Y., Lesieur, C. (2008-03). Trimeric reassembly of the globular domain of human C1q. Biochimica et Biophysica Acta - Proteins and Proteomics 1784 (3) : 518-529. ScholarBank@NUS Repository. https://doi.org/10.1016/j.bbapap.2007.12.005
dc.identifier.issn15709639
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/98458
dc.description.abstractC1q is a versatile recognition protein which binds to a variety of targets and consequently triggers the classical pathway of complement. C1q is a hetero-trimer composed of three chains (A, B and C) arranged in three domains, a short N-terminal region, followed by a collagenous repeat domain that gives rise to the formation of (ABC) triple helices, each ending in a C-terminal hetero-trimeric globular domain, called gC1q, which is responsible for the recognition properties of C1q. The mechanism of the trimeric assembly of C1q and in particular the role of each domain in the process is unknown. Here, we have investigated if the gC1q domain was able to assemble into functional trimers, in vitro, in the absence of the collagenous domain, a motif known to promote obligatory trimers in other proteins. Acid-mediated gC1q protomers reassembled into functional trimers, once neutralized, indicating that it is the gC1q domain which possesses the information for trimerization. However, reassembly occurred after neutralization, only if the gC1q protomers had preserved a residual tertiary structure at the end of the acidic treatment. Thus, the collagenous domain of C1q might initialize the folding of the gC1q domain so that subsequent assembly of the entire molecule can occur. © 2007.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1016/j.bbapap.2007.12.005
dc.sourceScopus
dc.subjectAssembly mechanism
dc.subjectC1q
dc.subjectFolding
dc.subjectFunction
dc.subjectTrimer
dc.typeArticle
dc.contributor.departmentPHYSICS
dc.description.doi10.1016/j.bbapap.2007.12.005
dc.description.sourcetitleBiochimica et Biophysica Acta - Proteins and Proteomics
dc.description.volume1784
dc.description.issue3
dc.description.page518-529
dc.description.codenBBAPB
dc.identifier.isiut000254780200011
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