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| {{STRUCTURE_1x79| PDB=1x79 | SCENE= }} | | {{STRUCTURE_1x79| PDB=1x79 | SCENE= }} |
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| '''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=== |
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| ==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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_15457209}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15457209 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15457209}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Intracellular trafficking]] | | [[Category: Intracellular trafficking]] |
| [[Category: Rabaptin5]] | | [[Category: Rabaptin5]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 14:39:28 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 15:47:53 2008'' |