Structural basis for acidic-cluster-dileucine sorting-signal recognition by VHS domains View Full Text


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Article Info

DATE

2002-02

AUTHORS

Saurav Misra, Rosa Puertollano, Yukio Kato, Juan S. Bonifacino, James H. Hurley

ABSTRACT

Specific sorting signals direct transmembrane proteins to the compartments of the endosomal–lysosomal system1. 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, γ-ear-containing, ADP-ribosylation-factor-binding) proteins2,3,4,5. The VHS (Vps27p, Hrs and STAM) domains6 of the GGA proteins are responsible for the highly specific recognition of these acidic-cluster-dileucine signals7,8,9,10. 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. More... »

PAGES

933-937

References to SciGraph publications

  • 2000-12. Peroxisomal targeting signal-1 recognition by the TPR domains of human PEX5 in NATURE STRUCTURAL & MOLECULAR BIOLOGY
  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/415933a

    DOI

    http://dx.doi.org/10.1038/415933a

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1023802018

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/11859375


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