1m23: Difference between revisions

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[[Image:1m23.gif|left|200px]]<br /><applet load="1m23" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1m23.gif|left|200px]]<br /><applet load="1m23" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1m23" />

'''STRUCTURE OF THE DIMERIZED CYTOPLASMIC DOMAIN OF P23 IN SOLUTION'''<br />

==Overview==

Coatomer, the coat protein complex of COPI vesicles, is involved in the, budding of these vesicles, but the underlying mechanism is unknown. Toward, a better understanding of this process, the interaction between coatomer, and the cytoplasmic domain of a major transmembrane protein of COPI, vesicles, p23, was studied. Interaction of coatomer with this peptide, domain results in a conformational change and polymerization of the, complex in vitro. This changed conformation also is observed in vivo, i.e., on the surface of authentic, isolated COPI vesicles. An average of, four peptides was found associated with one coatomer complex after, polymerization. Based on these results, we propose a mechanism by which, the induced conformational change of coatomer results in its, polymerization, and thus drives formation of the bud on the Golgi membrane, during biogenesis of a COPI vesicle.

Coatomer, the coat protein complex of COPI vesicles, is involved in the budding of these vesicles, but the underlying mechanism is unknown. Toward a better understanding of this process, the interaction between coatomer and the cytoplasmic domain of a major transmembrane protein of COPI vesicles, p23, was studied. Interaction of coatomer with this peptide domain results in a conformational change and polymerization of the complex in vitro. This changed conformation also is observed in vivo, i.e., on the surface of authentic, isolated COPI vesicles. An average of four peptides was found associated with one coatomer complex after polymerization. Based on these results, we propose a mechanism by which the induced conformational change of coatomer results in its polymerization, and thus drives formation of the bud on the Golgi membrane during biogenesis of a COPI vesicle.

==About this Structure==

1M23 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=1M23 OCA].

1M23 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=1M23 OCA].

==Reference==

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[[Category: vesicular transport]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20~~ 21:04:~~44 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:50:41 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1m23.gif|left|200px]]<br /><applet load="1m23" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1m23.gif|left|200px]]<br /><applet load="1m23" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1m23" />
 '''STRUCTURE OF THE DIMERIZED CYTOPLASMIC DOMAIN OF P23 IN SOLUTION'''<br />
 ==Overview==
-Coatomer, the coat protein complex of COPI vesicles, is involved in the, budding of these vesicles, but the underlying mechanism is unknown. Toward, a better understanding of this process, the interaction between coatomer, and the cytoplasmic domain of a major transmembrane protein of COPI, vesicles, p23, was studied. Interaction of coatomer with this peptide, domain results in a conformational change and polymerization of the, complex in vitro. This changed conformation also is observed in vivo, i.e., on the surface of authentic, isolated COPI vesicles. An average of, four peptides was found associated with one coatomer complex after, polymerization. Based on these results, we propose a mechanism by which, the induced conformational change of coatomer results in its, polymerization, and thus drives formation of the bud on the Golgi membrane, during biogenesis of a COPI vesicle.
+Coatomer, the coat protein complex of COPI vesicles, is involved in the budding of these vesicles, but the underlying mechanism is unknown. Toward a better understanding of this process, the interaction between coatomer and the cytoplasmic domain of a major transmembrane protein of COPI vesicles, p23, was studied. Interaction of coatomer with this peptide domain results in a conformational change and polymerization of the complex in vitro. This changed conformation also is observed in vivo, i.e., on the surface of authentic, isolated COPI vesicles. An average of four peptides was found associated with one coatomer complex after polymerization. Based on these results, we propose a mechanism by which the induced conformational change of coatomer results in its polymerization, and thus drives formation of the bud on the Golgi membrane during biogenesis of a COPI vesicle.
 ==About this Structure==
-M23 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=1M23 OCA].
+M23 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=1M23 OCA].
 ==Reference==
@@ Line 28: / Line 28: @@
 [[Category: vesicular transport]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:04:44 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:50:41 2008''