1naf: Difference between revisions
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'''crystal structure of the human GGA1 GAT domain''' | {{Structure | ||
|PDB= 1naf |SIZE=350|CAPTION= <scene name='initialview01'>1naf</scene>, resolution 2.80Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
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'''crystal structure of the human GGA1 GAT domain''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1NAF is a [ | 1NAF is a [[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== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12636914 12636914] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: three-helix bundle]] | [[Category: three-helix bundle]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:54:15 2008'' | ||
Revision as of 10:54, 20 March 2008
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| 1naf, resolution 2.80Å | |||||||||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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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