1f81

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(New page: 200px<br /><applet load="1f81" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f81" /> '''SOLUTION STRUCTURE OF THE TAZ2 DOMAIN OF THE...)
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[[Image:1f81.jpg|left|200px]]<br /><applet load="1f81" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1f81.jpg|left|200px]]<br /><applet load="1f81" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1f81" />
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'''SOLUTION STRUCTURE OF THE TAZ2 DOMAIN OF THE TRANSCRIPTIONAL ADAPTOR PROTEIN CBP'''<br />
'''SOLUTION STRUCTURE OF THE TAZ2 DOMAIN OF THE TRANSCRIPTIONAL ADAPTOR PROTEIN CBP'''<br />
==Overview==
==Overview==
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The TAZ2 (CH3) domain of the transcriptional adapter protein CBP has been, implicated in direct functional interactions with numerous cellular, transcription factors and viral oncoproteins. The solution structure of, the TAZ2 domain of murine CBP has been determined by nuclear magnetic, resonance (NMR). The protein adopts a novel helical fold stabilized by, three zinc ions, each of which is bound to one histidine and three, cysteine ligands in HCCC-type motifs. Each zinc-binding site is formed, from the carboxy terminus of an alpha-helix, a short loop, and the amino, terminus of the next alpha-helix. A peptide derived from the N-terminal, transactivation domain of p53 binds specifically to one face of the TAZ2, domain. The close similarities between the TAZ2 and TAZ1 (CH1 domain of, CBP/p300) sequences suggest that both domains will adopt similar, three-dimensional structures.
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The TAZ2 (CH3) domain of the transcriptional adapter protein CBP has been implicated in direct functional interactions with numerous cellular transcription factors and viral oncoproteins. The solution structure of the TAZ2 domain of murine CBP has been determined by nuclear magnetic resonance (NMR). The protein adopts a novel helical fold stabilized by three zinc ions, each of which is bound to one histidine and three cysteine ligands in HCCC-type motifs. Each zinc-binding site is formed from the carboxy terminus of an alpha-helix, a short loop, and the amino terminus of the next alpha-helix. A peptide derived from the N-terminal transactivation domain of p53 binds specifically to one face of the TAZ2 domain. The close similarities between the TAZ2 and TAZ1 (CH1 domain of CBP/p300) sequences suggest that both domains will adopt similar three-dimensional structures.
==About this Structure==
==About this Structure==
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1F81 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1F81 OCA].
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1F81 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F81 OCA].
==Reference==
==Reference==
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Dyson, H.J.]]
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[[Category: Dyson, H J.]]
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[[Category: Guzman, R.N.De.]]
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[[Category: Guzman, R N.De.]]
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[[Category: Liu, H.L.]]
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[[Category: Liu, H L.]]
[[Category: Martinez-Yamout, M.]]
[[Category: Martinez-Yamout, M.]]
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[[Category: Wright, P.E.]]
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[[Category: Wright, P E.]]
[[Category: ZN]]
[[Category: ZN]]
[[Category: cbp]]
[[Category: cbp]]
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[[Category: zinc finger]]
[[Category: zinc finger]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:41:48 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:35:52 2008''

Revision as of 10:35, 21 February 2008


1f81

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SOLUTION STRUCTURE OF THE TAZ2 DOMAIN OF THE TRANSCRIPTIONAL ADAPTOR PROTEIN CBP

Overview

The TAZ2 (CH3) domain of the transcriptional adapter protein CBP has been implicated in direct functional interactions with numerous cellular transcription factors and viral oncoproteins. The solution structure of the TAZ2 domain of murine CBP has been determined by nuclear magnetic resonance (NMR). The protein adopts a novel helical fold stabilized by three zinc ions, each of which is bound to one histidine and three cysteine ligands in HCCC-type motifs. Each zinc-binding site is formed from the carboxy terminus of an alpha-helix, a short loop, and the amino terminus of the next alpha-helix. A peptide derived from the N-terminal transactivation domain of p53 binds specifically to one face of the TAZ2 domain. The close similarities between the TAZ2 and TAZ1 (CH1 domain of CBP/p300) sequences suggest that both domains will adopt similar three-dimensional structures.

About this Structure

1F81 is a Single protein structure of sequence from Mus musculus with as ligand. Full crystallographic information is available from OCA.

Reference

Solution structure of the TAZ2 (CH3) domain of the transcriptional adaptor protein CBP., De Guzman RN, Liu HY, Martinez-Yamout M, Dyson HJ, Wright PE, J Mol Biol. 2000 Oct 20;303(2):243-53. PMID:11023789

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