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Recognition of accessory protein motifs by the gamma-adaptin ear domain of GGA3.

Nature structural biology | Aug 29, 2003

http://www.ncbi.nlm.nih.gov/pubmed/12858162

Adaptor proteins load transmembrane protein cargo into transport vesicles and serve as nexuses for the formation of large multiprotein complexes on the nascent vesicles. The gamma-adaptin ear (GAE) domains of the AP-1 adaptor protein complex and the GGA adaptor proteins recruit accessory proteins to these multiprotein complexes by binding to a hydrophobic motif. We determined the structure of the GAE domain of human GGA3 in complex with a peptide based on the DFGPLV sequence of the accessory protein Rabaptin-5 and refined it at a resolution of 2.2 A. The leucine and valine residues of the peptide are partly buried in two contiguous shallow, hydrophobic depressions. The anchoring phenylalanine is buried in a deep pocket formed by the aliphatic portions of two conserved arginine residues, along with an alanine and a proline, illustrating the unusual function of a cluster of basic residues in binding a hydrophobic motif.

Pubmed ID: 12858162 RIS Download

Mesh terms: ADP-Ribosylation Factors | Adaptor Protein Complex 1 | Adaptor Protein Complex gamma Subunits | Adaptor Proteins, Vesicular Transport | Amino Acid Sequence | Binding Sites | Carrier Proteins | Clathrin-Coated Vesicles | Crystallography, X-Ray | Humans | In Vitro Techniques | Macromolecular Substances | Models, Molecular | Molecular Sequence Data | Multiprotein Complexes | Protein Binding | Protein Structure, Tertiary | Sequence Homology, Amino Acid | Static Electricity | trans-Golgi Network

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