1naf: Difference between revisions

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[[Image:1naf.gif|left|200px]]
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{{STRUCTURE_1naf|  PDB=1naf  |  SCENE=  }}  
{{STRUCTURE_1naf|  PDB=1naf  |  SCENE=  }}  


'''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.
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{{ABSTRACT_PUBMED_12636914}}


==About this Structure==
==About this Structure==
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[[Category: Helical paper-clip]]
[[Category: Helical paper-clip]]
[[Category: Three-helix bundle]]
[[Category: Three-helix bundle]]
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Revision as of 11:45, 29 July 2008

File:1naf.png

Template:STRUCTURE 1naf

crystal structure of the human GGA1 GAT domain

Template:ABSTRACT PUBMED 12636914

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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