1x79: Difference between revisions

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[[Image:1x79.gif|left|200px]]
{{Seed}}
[[Image:1x79.png|left|200px]]


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{{STRUCTURE_1x79|  PDB=1x79  |  SCENE=  }}  
{{STRUCTURE_1x79|  PDB=1x79  |  SCENE=  }}  


'''Crystal structure of human GGA1 GAT domain complexed with the GAT-binding domain of Rabaptin5'''
===Crystal structure of human GGA1 GAT domain complexed with the GAT-binding domain of Rabaptin5===




==Overview==
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GGA proteins coordinate the intracellular trafficking of clathrin-coated vesicles through their interaction with several other proteins. The GAT domain of GGA proteins interacts with ARF, ubiquitin, and Rabaptin5. The GGA-Rabaptin5 interaction is believed to function in the fusion of trans-Golgi-derived vesicles to endosomes. We determined the crystal structure of a human GGA1 GAT domain fragment in complex with the Rabaptin5 GAT-binding domain. In this structure, the Rabaptin5 domain is a 90-residue-long helix. At the N-terminal end, it forms a parallel coiled-coil homodimer, which binds one GAT domain of GGA1. In the C-terminal region, it further assembles into a four-helix bundle tetramer. The Rabaptin5-binding motif of the GGA1 GAT domain consists of a three-helix bundle. Thus, the binding between Rabaptin5 and GGA1 GAT domain is based on a helix bundle-helix bundle interaction. The current structural observation is consistent with previously reported mutagenesis data, and its biological relevance is further confirmed by new mutagenesis studies and affinity analysis. The four-helix bundle structure of Rabaptin5 suggests a functional role in tethering organelles.
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{{ABSTRACT_PUBMED_15457209}}


==About this Structure==
==About this Structure==
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[[Category: Intracellular trafficking]]
[[Category: Intracellular trafficking]]
[[Category: Rabaptin5]]
[[Category: Rabaptin5]]
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