Please use this identifier to cite or link to this item: http://hdl.handle.net/2381/25978
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dc.contributor.authorKellenberger, E-
dc.contributor.authorDominguez, C-
dc.contributor.authorFribourg, S-
dc.contributor.authorWasielewski, E-
dc.contributor.authorMoras, D-
dc.contributor.authorPoterszman, A-
dc.contributor.authorBoelens, R-
dc.contributor.authorKieffer, B-
dc.date.accessioned2012-10-24T09:21:10Z-
dc.date.available2012-10-24T09:21:10Z-
dc.date.issued2005-5-27-
dc.identifier.citationJ BIOL CHEM, 2005, 280 (21), pp. 20785-20792-
dc.identifier.issn0021-9258-
dc.identifier.urihttp://hdl.handle.net/2381/25978-
dc.description.abstractThe human general transcription factor TFIIH is involved in both transcription and DNA nucleotide excision repair. Among the 10 subunits of the complex, p44 subunit plays a crucial role in both mechanisms. Its N-terminal domain interacts with the XPD helicase, whereas its C-terminal domain is involved specifically in the promoter escape activity. By mutating an exposed and non-conserved cysteine residue into a serine, we produced a soluble mutant of p44-(321-395) suitable for solution structure determination. The domain adopts a C4C4 RING domain structure with sequential organization of beta-strands that is related to canonical RING domains by a circular permutation of the beta-sheet elements. Analysis of the molecular surface and mutagenesis experiments suggests that the binding of p44-(321-395) to TFIIH p34 subunit is not mediated by electrostatic interactions and, thus, differs from previously reported interaction mechanisms involving RING domains.-
dc.formatmetadata-
dc.language.isoeng-
dc.sourcePubMed-
dc.source.urihttp://www.ncbi.nlm.nih.gov/pubmed/-
dc.subjectAmino Acid Sequence-
dc.subjectBinding Sites-
dc.subjectCysteine-
dc.subjectDNA-
dc.subjectComplementary-
dc.subjectEscherichia coli-
dc.subjectHumans-
dc.subjectMagnetic Resonance Spectroscopy-
dc.subjectModels-
dc.subjectMolecular-
dc.subjectMolecular Sequence Data-
dc.subjectMolecular Structure-
dc.subjectMutagenesis-
dc.subjectSite-Directed-
dc.subjectProtein Folding-
dc.subjectProtein Structure-
dc.subjectSecondary-
dc.subjectProtein Subunits-
dc.subjectRecombinant Proteins-
dc.subjectSequence Alignment-
dc.subjectSolutions-
dc.subjectTranscription Factor TFIIH-
dc.subjectTranscription Factors-
dc.subjectTFII-
dc.subjectTransfection-
dc.subjectZinc-
dc.titleSolution structure of the C-terminal domain of TFIIH P44 subunit reveals a novel type of C4C4 ring domain involved in protein-protein interactions.-
dc.typeJournal Article-
dc.identifier.doi10.1074/jbc.M412999200-
dc.identifier.piiM412999200-
dc.description.irispid86605-
Appears in Collections:Published Articles, Dept. of Biochemistry

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