1z60
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(New page: 200px<br /> <applet load="1z60" size="450" color="white" frame="true" align="right" spinBox="true" caption="1z60" /> '''Solution structure of the carboxy-terminal ...)
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Revision as of 18:23, 12 November 2007
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Solution structure of the carboxy-terminal domain of human TFIIH P44 subunit
Overview
The 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.
About this Structure
1Z60 is a Single protein structure of sequence from Homo sapiens with ZN as ligand. This structure superseeds the now removed PDB entry 1E53. Full crystallographic information is available from OCA.
Reference
Solution structure of the C-terminal domain of TFIIH P44 subunit reveals a novel type of C4C4 ring domain involved in protein-protein interactions., Kellenberger E, Dominguez C, Fribourg S, Wasielewski E, Moras D, Poterszman A, Boelens R, Kieffer B, J Biol Chem. 2005 May 27;280(21):20785-92. Epub 2005 Mar 24. PMID:15790571
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