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1naf

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[[Image:1naf.gif|left|200px]]<br /><applet load="1naf" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1naf.gif|left|200px]]
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caption="1naf, resolution 2.80&Aring;" />
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'''crystal structure of the human GGA1 GAT domain'''<br />
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{{Structure
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|PDB= 1naf |SIZE=350|CAPTION= <scene name='initialview01'>1naf</scene>, resolution 2.80&Aring;
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|SITE=
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|LIGAND=
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|ACTIVITY=
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}}
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'''crystal structure of the human GGA1 GAT domain'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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].
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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==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=12636914 12636914]
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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]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:03:58 2008''
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''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


PDB ID 1naf

Drag the structure with the mouse to rotate
, resolution 2.80Å
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

Page seeded by OCA on Thu Mar 20 12:54:15 2008

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