1tbo
From Proteopedia
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| - | [[Image:1tbo.jpg|left|200px]] | + | [[Image:1tbo.jpg|left|200px]] |
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| - | '''NMR STRUCTURE OF A PROTEIN KINASE C-G PHORBOL-BINDING DOMAIN, 30 STRUCTURES''' | + | {{Structure |
| + | |PDB= 1tbo |SIZE=350|CAPTION= <scene name='initialview01'>1tbo</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''NMR STRUCTURE OF A PROTEIN KINASE C-G PHORBOL-BINDING DOMAIN, 30 STRUCTURES''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1TBO is a [ | + | 1TBO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_rattus Rattus rattus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TBO OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9271501 9271501] |
[[Category: Rattus rattus]] | [[Category: Rattus rattus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:16:23 2008'' |
Revision as of 12:16, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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