1bh9: Difference between revisions
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==Overview== | ==Overview== | ||
Determination of the crystal structure of the human TBP-associated factor, (hTAF(II))28/hTAF(II)18 heterodimer shows that these TAF(II)s form a novel, histone-like pair in the TFIID complex. The histone folds in hTAF(II)28, and hTAF(II)18 were not predicted from their primary sequence, indicating, that these TAF(II)s define a novel family of atypical histone fold, sequences. The TAF(II)18 and TAF(II)28 histone fold motifs are also, present in the N- and C-terminal regions of the SPT3 proteins, suggesting, that the histone fold in SPT3 may be reconstituted by intramolecular, rather than classical intermolecular interactions. The existence of, additional histone-like pairs in both the TFIID and SAGA complexes shows, that the histone fold is a more commonly used motif for mediating TAF-TAF, . | Determination of the crystal structure of the human TBP-associated factor, (hTAF(II))28/hTAF(II)18 heterodimer shows that these TAF(II)s form a novel, histone-like pair in the TFIID complex. The histone folds in hTAF(II)28, and hTAF(II)18 were not predicted from their primary sequence, indicating, that these TAF(II)s define a novel family of atypical histone fold, sequences. The TAF(II)18 and TAF(II)28 histone fold motifs are also, present in the N- and C-terminal regions of the SPT3 proteins, suggesting, that the histone fold in SPT3 may be reconstituted by intramolecular, rather than classical intermolecular interactions. The existence of, additional histone-like pairs in both the TFIID and SAGA complexes shows, that the histone fold is a more commonly used motif for mediating TAF-TAF, interactions than previously believed. | ||
==About this Structure== | ==About this Structure== | ||
1BH9 is a | 1BH9 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with PMB as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: MRY. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BH9 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: transcription regulation complex]] | [[Category: transcription regulation complex]] | ||
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Revision as of 14:49, 5 November 2007
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HTAFII18/HTAFII28 HETERODIMER CRYSTAL STRUCTURE WITH BOUND PCMBS
OverviewOverview
Determination of the crystal structure of the human TBP-associated factor, (hTAF(II))28/hTAF(II)18 heterodimer shows that these TAF(II)s form a novel, histone-like pair in the TFIID complex. The histone folds in hTAF(II)28, and hTAF(II)18 were not predicted from their primary sequence, indicating, that these TAF(II)s define a novel family of atypical histone fold, sequences. The TAF(II)18 and TAF(II)28 histone fold motifs are also, present in the N- and C-terminal regions of the SPT3 proteins, suggesting, that the histone fold in SPT3 may be reconstituted by intramolecular, rather than classical intermolecular interactions. The existence of, additional histone-like pairs in both the TFIID and SAGA complexes shows, that the histone fold is a more commonly used motif for mediating TAF-TAF, interactions than previously believed.
About this StructureAbout this Structure
1BH9 is a Protein complex structure of sequences from Homo sapiens with PMB as ligand. Structure known Active Site: MRY. Full crystallographic information is available from OCA.
ReferenceReference
Human TAF(II)28 and TAF(II)18 interact through a histone fold encoded by atypical evolutionary conserved motifs also found in the SPT3 family., Birck C, Poch O, Romier C, Ruff M, Mengus G, Lavigne AC, Davidson I, Moras D, Cell. 1998 Jul 24;94(2):239-49. PMID:9695952
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