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| {{STRUCTURE_1om9| PDB=1om9 | SCENE= }} | | {{STRUCTURE_1om9| PDB=1om9 | SCENE= }} |
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| '''Structure of the GGA1-appendage in complex with the p56 binding peptide'''
| | ===Structure of the GGA1-appendage in complex with the p56 binding peptide=== |
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| ==Overview==
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| The Golgi-associated, gamma-adaptin-related, ADP-ribosylation-factor binding proteins (GGAs) and adaptor protein (AP)-1 are adaptors involved in clathrin-mediated transport between the trans-Golgi network and endosomal system. The appendage domains of GGAs and the AP-1 gamma-adaptin subunit are structurally homologous and have been proposed to bind to accessory proteins via interaction with short sequences containing phenylalanines and acidic residues. Here we present the structure of the human GGA1 appendage in complex with its cognate binding peptide from the p56 accessory protein (DDDDFGGFEAAETFD) as determined by X-ray crystallography. The interaction is governed predominantly by packing of the first two phenylalanine residues of the peptide with conserved basic and hydrophobic residues from GGA1. Additionally, several main chain hydrogen bonds cause the peptide to form an additional beta-strand on the edge of the preexisting beta-sheet of the protein. Isothermal titration calorimetry was used to assess the affinities of different peptides for the GGA and gamma-appendage domains. | | The line below this paragraph, {{ABSTRACT_PUBMED_12858163}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 12858163 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_12858163}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Clathrin adaptor]] | | [[Category: Clathrin adaptor]] |
| [[Category: Gga]] | | [[Category: Gga]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:01:30 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 19:57:58 2008'' |
