1ptr

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(New page: 200px<br /><applet load="1ptr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ptr, resolution 2.2&Aring;" /> '''PROTEIN KINASE C DELT...)
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[[Image:1ptr.gif|left|200px]]<br /><applet load="1ptr" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ptr.gif|left|200px]]<br /><applet load="1ptr" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ptr, resolution 2.2&Aring;" />
caption="1ptr, resolution 2.2&Aring;" />
'''PROTEIN KINASE C DELTA CYS2 DOMAIN COMPLEXED WITH PHORBOL-13-ACETATE'''<br />
'''PROTEIN KINASE C DELTA CYS2 DOMAIN COMPLEXED WITH PHORBOL-13-ACETATE'''<br />
==Overview==
==Overview==
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Protein kinase Cs (PKCs) are a ubiquitous family of regulatory enzymes, that associate with membranes and are activated by diacylglycerol or, tumor-promoting agonists such as phorbol esters. The structure of the, second activator-binding domain of PKC delta has been determined in, complex with phorbol 13-acetate, which binds in a groove between two, pulled-apart beta strands at the tip of the domain. The C3, C4, and C20, phorbol oxygens form hydrogen bonds with main-chain groups whose, orientation is controlled by a set of highly conserved residues. Phorbol, binding caps the groove and forms a contiguous hydrophobic surface, covering one-third of the domain, explaining how the activator promotes, insertion of PKC into membranes.
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Protein kinase Cs (PKCs) are a ubiquitous family of regulatory enzymes that associate with membranes and are activated by diacylglycerol or tumor-promoting agonists such as phorbol esters. The structure of the second activator-binding domain of PKC delta has been determined in complex with phorbol 13-acetate, which binds in a groove between two pulled-apart beta strands at the tip of the domain. The C3, C4, and C20 phorbol oxygens form hydrogen bonds with main-chain groups whose orientation is controlled by a set of highly conserved residues. Phorbol binding caps the groove and forms a contiguous hydrophobic surface covering one-third of the domain, explaining how the activator promotes insertion of PKC into membranes.
==About this Structure==
==About this Structure==
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1PTR 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 and PRB as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PTR OCA].
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1PTR 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> and <scene name='pdbligand=PRB:'>PRB</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PTR OCA].
==Reference==
==Reference==
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Hurley, J.H.]]
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[[Category: Hurley, J H.]]
[[Category: Zhang, G.]]
[[Category: Zhang, G.]]
[[Category: PRB]]
[[Category: PRB]]
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[[Category: phosphotransferase]]
[[Category: phosphotransferase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:07:14 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:32:31 2008''

Revision as of 12:32, 21 February 2008

Image:1ptr.gif

1ptr, resolution 2.2Å

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PROTEIN KINASE C DELTA CYS2 DOMAIN COMPLEXED WITH PHORBOL-13-ACETATE

Overview

Protein kinase Cs (PKCs) are a ubiquitous family of regulatory enzymes that associate with membranes and are activated by diacylglycerol or tumor-promoting agonists such as phorbol esters. The structure of the second activator-binding domain of PKC delta has been determined in complex with phorbol 13-acetate, which binds in a groove between two pulled-apart beta strands at the tip of the domain. The C3, C4, and C20 phorbol oxygens form hydrogen bonds with main-chain groups whose orientation is controlled by a set of highly conserved residues. Phorbol binding caps the groove and forms a contiguous hydrophobic surface covering one-third of the domain, explaining how the activator promotes insertion of PKC into membranes.

About this Structure

1PTR is a Single protein structure of sequence from Mus musculus with and as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of the cys2 activator-binding domain of protein kinase C delta in complex with phorbol ester., Zhang G, Kazanietz MG, Blumberg PM, Hurley JH, Cell. 1995 Jun 16;81(6):917-24. PMID:7781068

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