1ujk
From Proteopedia
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| - | [[Image:1ujk.gif|left|200px]] | + | [[Image:1ujk.gif|left|200px]] |
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| - | '''VHS domain of human GGA1 complexed with C-terminal phosphopeptide from BACE''' | + | {{Structure |
| + | |PDB= 1ujk |SIZE=350|CAPTION= <scene name='initialview01'>1ujk</scene>, resolution 1.9Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=IOD:IODIDE ION'>IOD</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''VHS domain of human GGA1 complexed with C-terminal phosphopeptide from BACE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1UJK is a [ | + | 1UJK is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UJK OCA]. |
==Reference== | ==Reference== | ||
| - | Insights into the phosphoregulation of beta-secretase sorting signal by the VHS domain of GGA1., Shiba T, Kametaka S, Kawasaki M, Shibata M, Waguri S, Uchiyama Y, Wakatsuki S, Traffic. 2004 Jun;5(6):437-48. PMID:[http:// | + | Insights into the phosphoregulation of beta-secretase sorting signal by the VHS domain of GGA1., Shiba T, Kametaka S, Kawasaki M, Shibata M, Waguri S, Uchiyama Y, Wakatsuki S, Traffic. 2004 Jun;5(6):437-48. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15117318 15117318] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: protein-peptide complex]] | [[Category: protein-peptide complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:32:47 2008'' |
Revision as of 12:32, 20 March 2008
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| , resolution 1.9Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
VHS domain of human GGA1 complexed with C-terminal phosphopeptide from BACE
Overview
BACE (beta-site amyloid precursor protein cleaving enzyme, beta-secretase) is a type-I membrane protein which functions as an aspartic protease in the production of beta-amyloid peptide, a causative agent of Alzheimer's disease. Its cytoplasmic tail has a characteristic acidic-cluster dileucine motif recognized by the VHS domain of adaptor proteins, GGAs (Golgi-localizing, gamma-adaptin ear homology domain, ARF-interacting). Here we show that BACE is colocalized with GGAs in the trans-Golgi network and peripheral structures, and phosphorylation of a serine residue in the cytoplasmic tail enhances interaction with the VHS domain of GGA1 by about threefold. The X-ray crystal structure of the complex between the GGA1-VHS domain and the BACE C-terminal peptide illustrates a similar recognition mechanism as mannose 6-phosphate receptors except that a glutamine residue closes in to fill the gap created by the shorter BACE peptide. The serine and lysine of the BACE peptide point their side chains towards the solvent. However, phosphorylation of the serine affects the lysine side chain and the peptide backbone, resulting in one additional hydrogen bond and a stronger electrostatic interaction with the VHS domain, hence the reversible increase in affinity.
About this Structure
1UJK is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Insights into the phosphoregulation of beta-secretase sorting signal by the VHS domain of GGA1., Shiba T, Kametaka S, Kawasaki M, Shibata M, Waguri S, Uchiyama Y, Wakatsuki S, Traffic. 2004 Jun;5(6):437-48. PMID:15117318
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