1jpl
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| , resolution 2.40Å | |||||||
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| Ligands: | |||||||
| Gene: | GGA3 (Homo sapiens) | ||||||
| Related: | 1ELK, 1DVP, 1juq
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
GGA3 VHS domain complexed with C-terminal peptide from cation-independent mannose 6-phosphate receptor
OverviewOverview
Specific sorting signals direct transmembrane proteins to the compartments of the endosomal-lysosomal system. Acidic-cluster-dileucine signals present within the cytoplasmic tails of sorting receptors, such as the cation-independent and cation-dependent mannose-6-phosphate receptors, are recognized by the GGA (Golgi-localized, gamma-ear-containing, ADP-ribosylation-factor-binding) proteins. The VHS (Vps27p, Hrs and STAM) domains of the GGA proteins are responsible for the highly specific recognition of these acidic-cluster-dileucine signals. Here we report the structures of the VHS domain of human GGA3 complexed with signals from both mannose-6-phosphate receptors. The signals bind in an extended conformation to helices 6 and 8 of the VHS domain. The structures highlight an Asp residue separated by two residues from a dileucine sequence as critical recognition elements. The side chains of the Asp-X-X-Leu-Leu sequence interact with subsites consisting of one electropositive and two shallow hydrophobic pockets, respectively. The rigid spatial alignment of the three binding subsites leads to high specificity.
About this StructureAbout this Structure
1JPL is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Structural basis for acidic-cluster-dileucine sorting-signal recognition by VHS domains., Misra S, Puertollano R, Kato Y, Bonifacino JS, Hurley JH, Nature. 2002 Feb 21;415(6874):933-7. PMID:11859375
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