1p23

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(New page: 200px<br /><applet load="1p23" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p23" /> '''STRUCTURE OF THE DIMERIZED CYTOPLASMIC DOMAI...)
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[[Image:1p23.gif|left|200px]]<br /><applet load="1p23" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1p23" />
caption="1p23" />
'''STRUCTURE OF THE DIMERIZED CYTOPLASMIC DOMAIN OF P23 IN SOLUTION, NMR, 10 STRUCTURES'''<br />
'''STRUCTURE OF THE DIMERIZED CYTOPLASMIC DOMAIN OF P23 IN SOLUTION, NMR, 10 STRUCTURES'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1P23 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1P23 OCA].
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1P23 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P23 OCA].
==Reference==
==Reference==
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[[Category: Roesch, P.]]
[[Category: Roesch, P.]]
[[Category: Weidler, M.]]
[[Category: Weidler, M.]]
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[[Category: Wieland, F.T.]]
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[[Category: Wieland, F T.]]
[[Category: coatomer]]
[[Category: coatomer]]
[[Category: cop]]
[[Category: cop]]
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[[Category: vesicular transport]]
[[Category: vesicular transport]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:24:02 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:24:13 2008''

Revision as of 12:24, 21 February 2008


1p23

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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 of sequence from [1]. 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

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