1tfb
From Proteopedia
(New page: 200px<br /> <applet load="1tfb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tfb" /> '''NMR STUDIES OF HUMAN GENERAL TRANSCRIPTION ...) |
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'''NMR STUDIES OF HUMAN GENERAL TRANSCRIPTION FACTOR TFIIB: DYNAMICS AND INTERACTION WITH VP16 ACTIVATION DOMAIN, 20 STRUCTURES'''<br /> | '''NMR STUDIES OF HUMAN GENERAL TRANSCRIPTION FACTOR TFIIB: DYNAMICS AND INTERACTION WITH VP16 ACTIVATION DOMAIN, 20 STRUCTURES'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1TFB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1TFB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TFB OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transcription factor]] | [[Category: transcription factor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:56:43 2008'' |
Revision as of 14:56, 15 February 2008
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NMR STUDIES OF HUMAN GENERAL TRANSCRIPTION FACTOR TFIIB: DYNAMICS AND INTERACTION WITH VP16 ACTIVATION DOMAIN, 20 STRUCTURES
Overview
Human TFIIB, an essential factor in transcription of protein-coding genes, by RNA polymerase II, consists of an amino-terminal zinc binding domain, (TFIIBn) connected by a linker of about 60 residues to a carboxy-terminal, core domain (TFIIBc). The TFIIB core domain has two internally repeated, motifs, each comprising five alpha-helices arranged as in the cyclin box., Compared to the crystal structure of TFIIBc in complex with TBP and a, TATA-containing oligonucleotide, the NMR-derived solution structure of, free TFIIBc is more compact, with a different repeat-repeat orientation, and a significantly shorter first helix in the second repeat. Analysis of, backbone 15N relaxation parameters indicates the presence of relatively, large amplitude, nanosecond time-scale motions in the TFIIBc interrepeat, linker and structural fluctuations throughout the backbone. Interaction of, TFIIBc with the acidic activation domain of VP16 or with TFIIBn induces, 1H-15N chemical shift and line width changes concentrated in the first, repeat, interrepeat linker and the first helix of the second repeat. These, results suggest that TFIIB is somewhat pliable and that the conformation, of the C-terminal core domain can be modulated by interaction with the, N-terminal zinc binding domain. Furthermore, binding of the VP16, activation domain may promote TFIIBc conformations primed for binding to a, TBP-DNA complex.
About this Structure
1TFB is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Human general transcription factor TFIIB: conformational variability and interaction with VP16 activation domain., Hayashi F, Ishima R, Liu D, Tong KI, Kim S, Reinberg D, Bagby S, Ikura M, Biochemistry. 1998 Jun 2;37(22):7941-51. PMID:9609687
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