1naf: Difference between revisions

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[[Image:1naf.~~gif~~|left|200px]]

[[Image:1naf.png|left|200px]]

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~~'''~~crystal structure of the human GGA1 GAT domain~~'''~~

===crystal structure of the human GGA1 GAT domain===

~~==Overview==~~

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The GGAs are a family of clathrin adaptor proteins involved in vesicular transport between the trans-Golgi network and endosomal system. Here we confirm reports that GGAs are targeted to the Golgi via interaction between the GGA-GAT domain and ARF-GTP, ~~and we present the structure of the GAT domain of human GGA1~~, ~~completing~~ the ~~structural description of~~ the ~~folded domains of GGA proteins~~. ~~The GGA-GAT domain possesses an all alpha-helical fold with a "paper clip" topology comprising two independent subdomains~~. ~~Structure-based mutagenesis demonstrates that ARF1-GTP binding by GGAs~~ is ~~exclusively governed by~~ the N-~~terminal "hook" subdomain, and, using an in vitro recruitment assay, we show that ARF~~-~~GTP binding by this small structure is required and sufficient for Golgi targeting of GGAs.~~

The line below this paragraph, {{ABSTRACT_PUBMED_12636914}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 12636914 is the PubMed ID number.

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==About this Structure==

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[[Category: Helical paper-clip]]

[[Category: Three-helix bundle]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 02~~:17:30 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 14:45:11 2008''

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-[[Image:1naf.gif|left|200px]]
+{{Seed}}
+[[Image:1naf.png|left|200px]]
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 {{STRUCTURE_1naf|  PDB=1naf  |  SCENE=  }}
-'''crystal structure of the human GGA1 GAT domain'''
+===crystal structure of the human GGA1 GAT domain===
-==Overview==
+<!--
-The GGAs are a family of clathrin adaptor proteins involved in vesicular transport between the trans-Golgi network and endosomal system. Here we confirm reports that GGAs are targeted to the Golgi via interaction between the GGA-GAT domain and ARF-GTP, and we present the structure of the GAT domain of human GGA1, completing the structural description of the folded domains of GGA proteins. The GGA-GAT domain possesses an all alpha-helical fold with a "paper clip" topology comprising two independent subdomains. Structure-based mutagenesis demonstrates that ARF1-GTP binding by GGAs is exclusively governed by the N-terminal "hook" subdomain, and, using an in vitro recruitment assay, we show that ARF-GTP binding by this small structure is required and sufficient for Golgi targeting of GGAs.
+The line below this paragraph, {{ABSTRACT_PUBMED_12636914}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12636914 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12636914}}
 ==About this Structure==
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 [[Category: Helical paper-clip]]
 [[Category: Three-helix bundle]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 02:17:30 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 14:45:11 2008''