1tbo
From Proteopedia
(New page: 200px<br /><applet load="1tbo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tbo" /> '''NMR STRUCTURE OF A PROTEIN KINASE C-G PHORBO...) |
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| - | [[Image:1tbo.jpg|left|200px]]<br /><applet load="1tbo" size=" | + | [[Image:1tbo.jpg|left|200px]]<br /><applet load="1tbo" size="350" color="white" frame="true" align="right" spinBox="true" |
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'''NMR STRUCTURE OF A PROTEIN KINASE C-G PHORBOL-BINDING DOMAIN, 30 STRUCTURES'''<br /> | '''NMR STRUCTURE OF A PROTEIN KINASE C-G PHORBOL-BINDING DOMAIN, 30 STRUCTURES'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Classical protein kinase C (PKC) family members are activated by the | + | Classical protein kinase C (PKC) family members are activated by the binding of various ligands to one of several cysteine-rich domains of the enzyme. The natural agonist, diacylglycerol (DAG), and the natural product superagonist, phorbol dibutyrate (PDB), activate the enzyme to produce wide-ranging physiological effects. The second cysteine-rich (Cys2) domain of rat brain PKC-gamma was expressed and labeled with 15N and 13C, and the solution structure was determined to high resolution using multidimensional heteronuclear NMR methods. The phorbol binding site was identified by titrating this domain with phorbol-12,13-dibutyrate (PDB) in the presence of organic cosolvents. Titrations of this domain with lipid micelles, in the absence and presence of phorbols, indicate selective broadening of some resonances. The observed behavior indicates conformational exchange between bound and free states upon protein-micelle interaction. The data also suggest that half of the domain, including the phorbol site and one of the zinc sites, is capable of inserting into membranes. |
==About this Structure== | ==About this Structure== | ||
| - | 1TBO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_rattus Rattus rattus] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1TBO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_rattus Rattus rattus] 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=1TBO OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Rattus rattus]] | [[Category: Rattus rattus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Brown, S | + | [[Category: Brown, S C.]] |
[[Category: Pawelczyk, T.]] | [[Category: Pawelczyk, T.]] | ||
[[Category: Xia, T.]] | [[Category: Xia, T.]] | ||
| - | [[Category: Xu, R | + | [[Category: Xu, R X.]] |
[[Category: ZN]] | [[Category: ZN]] | ||
[[Category: calcium-binding protein]] | [[Category: calcium-binding protein]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:11:55 2008'' |
Revision as of 13:11, 21 February 2008
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NMR STRUCTURE OF A PROTEIN KINASE C-G PHORBOL-BINDING DOMAIN, 30 STRUCTURES
Overview
Classical protein kinase C (PKC) family members are activated by the binding of various ligands to one of several cysteine-rich domains of the enzyme. The natural agonist, diacylglycerol (DAG), and the natural product superagonist, phorbol dibutyrate (PDB), activate the enzyme to produce wide-ranging physiological effects. The second cysteine-rich (Cys2) domain of rat brain PKC-gamma was expressed and labeled with 15N and 13C, and the solution structure was determined to high resolution using multidimensional heteronuclear NMR methods. The phorbol binding site was identified by titrating this domain with phorbol-12,13-dibutyrate (PDB) in the presence of organic cosolvents. Titrations of this domain with lipid micelles, in the absence and presence of phorbols, indicate selective broadening of some resonances. The observed behavior indicates conformational exchange between bound and free states upon protein-micelle interaction. The data also suggest that half of the domain, including the phorbol site and one of the zinc sites, is capable of inserting into membranes.
About this Structure
1TBO is a Single protein structure of sequence from Rattus rattus with as ligand. Full crystallographic information is available from OCA.
Reference
NMR structure of a protein kinase C-gamma phorbol-binding domain and study of protein-lipid micelle interactions., Xu RX, Pawelczyk T, Xia TH, Brown SC, Biochemistry. 1997 Sep 2;36(35):10709-17. PMID:9271501
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