1naf
From Proteopedia
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[[Image:1naf.gif|left|200px]] | [[Image:1naf.gif|left|200px]] | ||
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'''crystal structure of the human GGA1 GAT domain''' | '''crystal structure of the human GGA1 GAT domain''' | ||
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[[Category: Owen, D J.]] | [[Category: Owen, D J.]] | ||
[[Category: Watson, P J.]] | [[Category: Watson, P J.]] | ||
| - | [[Category: | + | [[Category: Clathrin-adaptor]] |
| - | [[Category: | + | [[Category: Gat domain]] |
| - | [[Category: | + | [[Category: Gga]] |
| - | [[Category: | + | [[Category: Helical paper-clip]] |
| - | [[Category: | + | [[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 | + | |
Revision as of 23:17, 2 May 2008
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 Page seeded by OCA on Sat May 3 02:17:30 2008
