1naf
From Proteopedia
(New page: 200px<br /> <applet load="1naf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1naf, resolution 2.80Å" /> '''crystal structure o...) |
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| - | [[Image:1naf.gif|left|200px]]<br /> | + | [[Image:1naf.gif|left|200px]]<br /><applet load="1naf" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1naf" size=" | + | |
caption="1naf, resolution 2.80Å" /> | caption="1naf, resolution 2.80Å" /> | ||
'''crystal structure of the human GGA1 GAT domain'''<br /> | '''crystal structure of the human GGA1 GAT domain'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The GGAs are a family of clathrin adaptor proteins involved in vesicular | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1NAF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1NAF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NAF OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Collins, B | + | [[Category: Collins, B M.]] |
| - | [[Category: Owen, D | + | [[Category: Owen, D J.]] |
| - | [[Category: Watson, P | + | [[Category: Watson, P J.]] |
[[Category: clathrin-adaptor]] | [[Category: clathrin-adaptor]] | ||
[[Category: gat domain]] | [[Category: gat domain]] | ||
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[[Category: three-helix bundle]] | [[Category: three-helix bundle]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:03:58 2008'' |
Revision as of 12:03, 21 February 2008
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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.
About this Structure
1NAF is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The structure of the GGA1-GAT domain reveals the molecular basis for ARF binding and membrane association of GGAs., Collins BM, Watson PJ, Owen DJ, Dev Cell. 2003 Mar;4(3):321-32. PMID:12636914
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