1na8

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[[Image:1na8.jpg|left|200px]]
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{{Structure
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{{STRUCTURE_1na8| PDB=1na8 | SCENE= }}
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|RELATEDENTRY=[[1gyu|1GYU]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1na8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1na8 OCA], [http://www.ebi.ac.uk/pdbsum/1na8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1na8 RCSB]</span>
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'''Crystal structure of ADP-ribosylation factor binding protein GGA1'''
'''Crystal structure of ADP-ribosylation factor binding protein GGA1'''
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[[Category: Robinson, M S.]]
[[Category: Robinson, M S.]]
[[Category: Schu, P.]]
[[Category: Schu, P.]]
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[[Category: appendage]]
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[[Category: Appendage]]
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[[Category: beta-sandwich]]
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[[Category: Beta-sandwich]]
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[[Category: clathrin-adaptor]]
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[[Category: Clathrin-adaptor]]
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[[Category: gga]]
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[[Category: Gga]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:17:17 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:27:36 2008''
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Revision as of 23:17, 2 May 2008

Image:1na8.jpg

Template:STRUCTURE 1na8

Crystal structure of ADP-ribosylation factor binding protein GGA1


Overview

The adaptor appendage domains are believed to act as binding platforms for coated vesicle accessory proteins. Using glutathione S-transferase pulldowns from pig brain cytosol, we find three proteins that can bind to the appendage domains of both the AP-1 gamma subunit and the GGAs: gamma-synergin and two novel proteins, p56 and p200. p56 elicited better antibodies than p200 and was generally more tractable. Although p56 and gamma-synergin bind to both GGA and gamma appendages in vitro, immunofluorescence labeling of nocodazole-treated cells shows that p56 colocalizes with GGAs on TGN46-positive membranes, whereas gamma-synergin colocalizes with AP-1 primarily on a different membrane compartment. Furthermore, in AP-1-deficient cells, p56 remains membrane-associated whereas gamma-synergin becomes cytosolic. Thus, p56 and gamma-synergin show very strong preferences for GGAs and AP-1, respectively, in vivo. However, the GGA and gamma appendages share the same fold as determined by x-ray crystallography, and mutagenesis reveals that the same amino acids contribute to their binding sites. By overexpressing wild-type GGA and gamma appendage domains in cells, we can drive p56 and gamma-synergin, respectively, into the cytosol, suggesting a possible mechanism for selectively disrupting the two pathways.

About this Structure

1NA8 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Binding partners for the COOH-terminal appendage domains of the GGAs and gamma-adaptin., Lui WW, Collins BM, Hirst J, Motley A, Millar C, Schu P, Owen DJ, Robinson MS, Mol Biol Cell. 2003 Jun;14(6):2385-98. Epub 2003 Mar 20. PMID:12808037 Page seeded by OCA on Sat May 3 02:17:17 2008

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