| pubmed-article:15701688 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15701688 | lifeskim:mentions | umls-concept:C0524637 | lld:lifeskim |
| pubmed-article:15701688 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:15701688 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:15701688 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:15701688 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:15701688 | pubmed:dateCreated | 2005-2-16 | lld:pubmed |
| pubmed-article:15701688 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15701688 | pubmed:abstractText | The Golgi-localized, gamma-ear-containing, Arf (ADP-ribosylation factor)-binding (GGA) proteins are clathrin adaptors that mediate the sorting of transmembrane-cargo molecules at the trans-Golgi network and endosomes. Cargo proteins can be directed into the GGA pathway by at least two different types of sorting signals: acidic cluster-dileucine motifs and covalent modification by ubiquitin. The latter modification is recognized by the GGAs through binding to their GAT [GGA and TOM (target of Myb)] domain. Here we report the crystal structure of the GAT domain of human GGA3 in a 1:1 complex with ubiquitin at 2.8-A resolution. Ubiquitin binds to a hydrophobic and acidic patch on helices alpha1 and alpha2 of the GAT three-helix bundle that includes Asn-223, Leu-227, Glu-230, Met-231, Asp-244, Glu-246, Leu-247, Glu-250, and Leu-251. The GAT-binding surface on ubiquitin is a hydrophobic patch centered on Ile-44 that is also responsible for binding most other ubiquitin effectors. The ubiquitin-binding site observed in the crystal is distinct from the Rabaptin-5-binding site on helices alpha2 and alpha3 of the GAT domain. Mutational analysis and modeling of the ubiquitin-Rabaptin-5-GAT ternary complex indicates that ubiquitin and Rabaptin-5 can bind to the GAT domain at two different sites without any steric conflict. This ability highlights the GAT domain as a hub for interactions with multiple partners in trafficking. | lld:pubmed |
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| pubmed-article:15701688 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15701688 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15701688 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15701688 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:15701688 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15701688 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:15701688 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:15701688 | pubmed:author | pubmed-author:BonifacinoJua... | lld:pubmed |
| pubmed-article:15701688 | pubmed:author | pubmed-author:HurleyJames... | lld:pubmed |
| pubmed-article:15701688 | pubmed:author | pubmed-author:LeeSanghoS | lld:pubmed |
| pubmed-article:15701688 | pubmed:author | pubmed-author:BeachBridgett... | lld:pubmed |
| pubmed-article:15701688 | pubmed:author | pubmed-author:MatteraRafael... | lld:pubmed |
| pubmed-article:15701688 | pubmed:author | pubmed-author:ArighiCecilia... | lld:pubmed |
| pubmed-article:15701688 | pubmed:author | pubmed-author:PragGaliG | lld:pubmed |
| pubmed-article:15701688 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15701688 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:15701688 | pubmed:volume | 102 | lld:pubmed |
| pubmed-article:15701688 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15701688 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15701688 | pubmed:pagination | 2334-9 | lld:pubmed |
| pubmed-article:15701688 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:15701688 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:15701688 | pubmed:articleTitle | Structural mechanism for ubiquitinated-cargo recognition by the Golgi-localized, gamma-ear-containing, ADP-ribosylation-factor-binding proteins. | lld:pubmed |
| pubmed-article:15701688 | pubmed:affiliation | Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA. | lld:pubmed |
| pubmed-article:15701688 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15701688 | pubmed:publicationType | In Vitro | lld:pubmed |
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