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2nxp

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(New page: 200px<br /> <applet load="2nxp" size="450" color="white" frame="true" align="right" spinBox="true" caption="2nxp, resolution 2.17&Aring;" /> '''Structure of NTD2 d...)
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[[Image:2nxp.gif|left|200px]]<br />
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[[Image:2nxp.gif|left|200px]]<br /><applet load="2nxp" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="2nxp" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="2nxp, resolution 2.17&Aring;" />
caption="2nxp, resolution 2.17&Aring;" />
'''Structure of NTD2 domain of the human TAF5 subunit of TFIID'''<br />
'''Structure of NTD2 domain of the human TAF5 subunit of TFIID'''<br />
==Overview==
==Overview==
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TFIID is an essential factor required for RNA polymerase II transcription, but remains poorly understood because of its intrinsic complexity. Human, TAF5, a 100-kDa subunit of general transcription factor TFIID, is an, essential gene and plays a critical role in assembling the 1.2 MDa TFIID, complex. We report here a structural analysis of the TAF5 protein. Our, structure at 2.2-A resolution of the TAF5-NTD2 domain reveals an, alpha-helical domain with distant structural similarity to RNA polymerase, II CTD interacting factors. The TAF5-NTD2 domain contains several, conserved clefts likely to be critical for TFIID complex assembly. Our, biochemical analysis of the human TAF5 protein demonstrates the ability of, the N-terminal half of the TAF5 gene to form a flexible, extended dimer, a, key property required for the assembly of the TFIID complex.
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TFIID is an essential factor required for RNA polymerase II transcription but remains poorly understood because of its intrinsic complexity. Human TAF5, a 100-kDa subunit of general transcription factor TFIID, is an essential gene and plays a critical role in assembling the 1.2 MDa TFIID complex. We report here a structural analysis of the TAF5 protein. Our structure at 2.2-A resolution of the TAF5-NTD2 domain reveals an alpha-helical domain with distant structural similarity to RNA polymerase II CTD interacting factors. The TAF5-NTD2 domain contains several conserved clefts likely to be critical for TFIID complex assembly. Our biochemical analysis of the human TAF5 protein demonstrates the ability of the N-terminal half of the TAF5 gene to form a flexible, extended dimer, a key property required for the assembly of the TFIID complex.
==About this Structure==
==About this Structure==
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2NXP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2NXP OCA].
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2NXP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NXP OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Bhattacharya, S.]]
[[Category: Bhattacharya, S.]]
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[[Category: Jacobson, R.H.]]
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[[Category: Jacobson, R H.]]
[[Category: Takada, S.]]
[[Category: Takada, S.]]
[[Category: CA]]
[[Category: CA]]
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[[Category: transcription factor]]
[[Category: transcription factor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 23:03:42 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:12:09 2008''

Revision as of 16:12, 21 February 2008

Image:2nxp.gif

2nxp, resolution 2.17Å

Drag the structure with the mouse to rotate

Structure of NTD2 domain of the human TAF5 subunit of TFIID

Overview

TFIID is an essential factor required for RNA polymerase II transcription but remains poorly understood because of its intrinsic complexity. Human TAF5, a 100-kDa subunit of general transcription factor TFIID, is an essential gene and plays a critical role in assembling the 1.2 MDa TFIID complex. We report here a structural analysis of the TAF5 protein. Our structure at 2.2-A resolution of the TAF5-NTD2 domain reveals an alpha-helical domain with distant structural similarity to RNA polymerase II CTD interacting factors. The TAF5-NTD2 domain contains several conserved clefts likely to be critical for TFIID complex assembly. Our biochemical analysis of the human TAF5 protein demonstrates the ability of the N-terminal half of the TAF5 gene to form a flexible, extended dimer, a key property required for the assembly of the TFIID complex.

About this Structure

2NXP is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

Structural analysis and dimerization potential of the human TAF5 subunit of TFIID., Bhattacharya S, Takada S, Jacobson RH, Proc Natl Acad Sci U S A. 2007 Jan 23;104(4):1189-94. Epub 2007 Jan 16. PMID:17227857

Page seeded by OCA on Thu Feb 21 18:12:09 2008

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