1kbh: Difference between revisions

Revision as of 10:05, 2 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1kbh.png

Template:STRUCTURE 1kbh

Mutual Synergistic Folding in the Interaction Between Nuclear Receptor Coactivators CBP and ACTRMutual Synergistic Folding in the Interaction Between Nuclear Receptor Coactivators CBP and ACTR

Template:ABSTRACT PUBMED 11823864

About this StructureAbout this Structure

1KBH is a Protein complex structure of sequences from Homo sapiens and Mus musculus. Full experimental information is available from OCA.

ReferenceReference

Mutual synergistic folding in recruitment of CBP/p300 by p160 nuclear receptor coactivators., Demarest SJ, Martinez-Yamout M, Chung J, Chen H, Xu W, Dyson HJ, Evans RM, Wright PE, Nature. 2002 Jan 31;415(6871):549-53. PMID:11823864

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Mutual Synergistic Folding in the Interaction Between Nuclear Receptor Coactivators CBP and ACTR'''
+===Mutual Synergistic Folding in the Interaction Between Nuclear Receptor Coactivators CBP and ACTR===
-==Overview==
+<!--
-Nuclear hormone receptors are ligand-activated transcription factors that regulate the expression of genes that are essential for development, reproduction and homeostasis. The hormone response is mediated through recruitment of p160 receptor coactivators and the general transcriptional coactivator CBP/p300, which function synergistically to activate transcription. These coactivators exhibit intrinsic histone acetyltransferase activity, function in the remodelling of chromatin, and facilitate the recruitment of RNA polymerase II and the basal transcription machinery. The activities of the p160 coactivators are dependent on CBP. Both coactivators are essential for proper cell-cycle control, differentiation and apoptosis, and are implicated in cancer and other diseases. To elucidate the molecular basis of assembling the multiprotein activation complex, we undertook a structural and thermodynamic analysis of the interaction domains of CBP and the activator for thyroid hormone and retinoid receptors. Here we show that although the isolated domains are intrinsically disordered, they combine with high affinity to form a cooperatively folded helical heterodimer. Our study uncovers a unique mechanism, called 'synergistic folding', through which p160 coactivators recruit CBP/p300 to allow transmission of the hormonal signal to the transcriptional machinery.
+The line below this paragraph, {{ABSTRACT_PUBMED_11823864}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11823864 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_11823864}}
 ==About this Structure==
-KBH is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KBH OCA].
+KBH is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KBH OCA].
 ==Reference==
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 [[Category: P160]]
 [[Category: P300]]
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