1p23
From Proteopedia
STRUCTURE OF THE DIMERIZED CYTOPLASMIC DOMAIN OF P23 IN SOLUTION, NMR, 10 STRUCTURES
Overview
Coatomer, the coat protein complex of coat protein (COPI) vesicles, is involved in the budding of these vesicles. Its interaction with the cytoplasmic domains of some p24-family members, type I transmembrane proteins of the Golgi, has been shown to induce a conformational change of coatomer that initiates polymerization of the complex. From stoichiometrical data it is likely that interaction of coatomer with the small tail domains involves an oligomeric form of the p24 proteins. Here we present the structure of peptide analogs of the cytoplasmic domain of p23, a member of the p24 family, as determined by two-dimensional nuclear magnetic resonance spectroscopy in the presence of 2,2,2-trifluoroethanol. An improved strategy for structure calculation revealed that the tail domain peptides form alpha-helices and adopt a tetrameric state. Based on these results we propose an initial model for the binding of coatomer by p23 and the induced conformational change of coatomer that results in its polymerization, curvature of the Golgi membrane to form a bud, and finally a COPI-coated vesicle.
About this Structure
1P23 is a Single protein structure. Full crystallographic information is available from OCA.
Reference
Structure of the cytoplasmic domain of p23 in solution: implications for the formation of COPI vesicles., Weidler M, Reinhard C, Friedrich G, Wieland FT, Rosch P, Biochem Biophys Res Commun. 2000 May 10;271(2):401-8. PMID:10799309 Page seeded by OCA on Sat May 3 04:34:59 2008
