1om9
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The Golgi-associated, gamma-adaptin-related, ADP-ribosylation-factor | + | 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. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Collins, B | + | [[Category: Collins, B M.]] |
| - | [[Category: Owen, D | + | [[Category: Owen, D J.]] |
| - | [[Category: Praefcke, G | + | [[Category: Praefcke, G J.K.]] |
| - | [[Category: Robinson, M | + | [[Category: Robinson, M S.]] |
[[Category: adaptin]] | [[Category: adaptin]] | ||
[[Category: beta augmentation]] | [[Category: beta augmentation]] | ||
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[[Category: gga]] | [[Category: gga]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:19:14 2008'' |
Revision as of 12:19, 21 February 2008
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Structure of the GGA1-appendage in complex with the p56 binding peptide
Overview
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.
About this Structure
1OM9 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural basis for binding of accessory proteins by the appendage domain of GGAs., Collins BM, Praefcke GJ, Robinson MS, Owen DJ, Nat Struct Biol. 2003 Aug;10(8):607-13. PMID:12858163
Page seeded by OCA on Thu Feb 21 14:19:14 2008
