1r4x: Difference between revisions

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==Overview==

COPI-coated vesicles mediate retrograde transport from the Golgi back to, the ER and intra-Golgi transport. The cytosolic precursor of the COPI, coat, the heptameric coatomer complex, can be thought of as composed of, two subcomplexes. The first consists of the beta-, gamma-, delta- and, zeta-COP subunits which are distantly homologous to AP clathrin adaptor, subunits. The second consists of the alpha-, beta'- and epsilon-COP, subunits. Here, we present the structure of the appendage domain of, gamma-COP and show that it has a similar overall fold as the, alpha-appendage of AP2. Again, like the alpha-appendage the gamma-COP, appendage possesses a single protein/protein interaction site on its, platform subdomain. We show that in yeast this site binds to the ARFGAP, Glo3p, and in mammalian gamma-COP this site binds to a Glo3p orthologue, ARFGAP2. On the basis of mutations in the yeast homologue of gamma-COP, Sec21p, a second binding site is proposed to exist on the gamma-COP, appendage that interacts with the alpha,beta',epsilon COPI subcomplex.

COPI-coated vesicles mediate retrograde transport from the Golgi back to the ER and intra-Golgi transport. The cytosolic precursor of the COPI coat, the heptameric coatomer complex, can be thought of as composed of two subcomplexes. The first consists of the beta-, gamma-, delta- and zeta-COP subunits which are distantly homologous to AP clathrin adaptor subunits. The second consists of the alpha-, beta'- and epsilon-COP subunits. Here, we present the structure of the appendage domain of gamma-COP and show that it has a similar overall fold as the alpha-appendage of AP2. Again, like the alpha-appendage the gamma-COP appendage possesses a single protein/protein interaction site on its platform subdomain. We show that in yeast this site binds to the ARFGAP Glo3p, and in mammalian gamma-COP this site binds to a Glo3p orthologue, ARFGAP2. On the basis of mutations in the yeast homologue of gamma-COP, Sec21p, a second binding site is proposed to exist on the gamma-COP appendage that interacts with the alpha,beta',epsilon COPI subcomplex.

==About this Structure==

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[[Category: Homo sapiens]]

[[Category: Single protein]]

[[Category: Collins, B.M.]]

[[Category: Collins, B M.]]

[[Category: Duden, R.]]

[[Category: Frigerio, G.]]

[[Category: Owen, D.J.]]

[[Category: Owen, D J.]]

[[Category: Watson, P.J.]]

[[Category: Watson, P J.]]

[[Category: MG]]

[[Category: appendage; beta sandwich; coatomer; adp-ribosylation factors]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri~~ Feb ~~15 16~~:46:55 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:47:06 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-COPI-coated vesicles mediate retrograde transport from the Golgi back to, the ER and intra-Golgi transport. The cytosolic precursor of the COPI, coat, the heptameric coatomer complex, can be thought of as composed of, two subcomplexes. The first consists of the beta-, gamma-, delta- and, zeta-COP subunits which are distantly homologous to AP clathrin adaptor, subunits. The second consists of the alpha-, beta'- and epsilon-COP, subunits. Here, we present the structure of the appendage domain of, gamma-COP and show that it has a similar overall fold as the, alpha-appendage of AP2. Again, like the alpha-appendage the gamma-COP, appendage possesses a single protein/protein interaction site on its, platform subdomain. We show that in yeast this site binds to the ARFGAP, Glo3p, and in mammalian gamma-COP this site binds to a Glo3p orthologue, ARFGAP2. On the basis of mutations in the yeast homologue of gamma-COP, Sec21p, a second binding site is proposed to exist on the gamma-COP, appendage that interacts with the alpha,beta',epsilon COPI subcomplex.
+COPI-coated vesicles mediate retrograde transport from the Golgi back to the ER and intra-Golgi transport. The cytosolic precursor of the COPI coat, the heptameric coatomer complex, can be thought of as composed of two subcomplexes. The first consists of the beta-, gamma-, delta- and zeta-COP subunits which are distantly homologous to AP clathrin adaptor subunits. The second consists of the alpha-, beta'- and epsilon-COP subunits. Here, we present the structure of the appendage domain of gamma-COP and show that it has a similar overall fold as the alpha-appendage of AP2. Again, like the alpha-appendage the gamma-COP appendage possesses a single protein/protein interaction site on its platform subdomain. We show that in yeast this site binds to the ARFGAP Glo3p, and in mammalian gamma-COP this site binds to a Glo3p orthologue, ARFGAP2. On the basis of mutations in the yeast homologue of gamma-COP, Sec21p, a second binding site is proposed to exist on the gamma-COP appendage that interacts with the alpha,beta',epsilon COPI subcomplex.
 ==About this Structure==
@@ Line 13: / Line 13: @@
 [[Category: Homo sapiens]]
 [[Category: Single protein]]
-[[Category: Collins, B.M.]]
+[[Category: Collins, B M.]]
 [[Category: Duden, R.]]
 [[Category: Frigerio, G.]]
-[[Category: Owen, D.J.]]
+[[Category: Owen, D J.]]
-[[Category: Watson, P.J.]]
+[[Category: Watson, P J.]]
 [[Category: MG]]
 [[Category: appendage; beta sandwich; coatomer; adp-ribosylation factors]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:46:55 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:47:06 2008''