1naf
From Proteopedia
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|PDB= 1naf |SIZE=350|CAPTION= <scene name='initialview01'>1naf</scene>, resolution 2.80Å | |PDB= 1naf |SIZE=350|CAPTION= <scene name='initialview01'>1naf</scene>, resolution 2.80Å | ||
|SITE= | |SITE= | ||
- | |LIGAND= | + | |LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY=[[1gyu|1GYU]] | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1naf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1naf OCA], [http://www.ebi.ac.uk/pdbsum/1naf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1naf RCSB]</span> | ||
}} | }} | ||
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[[Category: three-helix bundle]] | [[Category: three-helix bundle]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:27:34 2008'' |
Revision as of 19:27, 30 March 2008
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, resolution 2.80Å | |||||||
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Ligands: | |||||||
Related: | 1GYU
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Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
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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