1tbo
From Proteopedia
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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 ZN 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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