Ontology type: schema:ScholarlyArticle
2002-02
AUTHORSSaurav Misra, Rosa Puertollano, Yukio Kato, Juan S. Bonifacino, James H. Hurley
ABSTRACTSpecific 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... »
PAGES933-937
http://scigraph.springernature.com/pub.10.1038/415933a
DOIhttp://dx.doi.org/10.1038/415933a
DIMENSIONShttps://app.dimensions.ai/details/publication/pub.1023802018
PUBMEDhttps://www.ncbi.nlm.nih.gov/pubmed/11859375
JSON-LD is the canonical representation for SciGraph data.
TIP: You can open this SciGraph record using an external JSON-LD service: JSON-LD Playground Google SDTT
[
{
"@context": "https://springernature.github.io/scigraph/jsonld/sgcontext.json",
"about": [
{
"id": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/06",
"inDefinedTermSet": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/",
"name": "Biological Sciences",
"type": "DefinedTerm"
},
{
"id": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/0601",
"inDefinedTermSet": "http://purl.org/au-research/vocabulary/anzsrc-for/2008/",
"name": "Biochemistry and Cell Biology",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "ADP-Ribosylation Factors",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "Adaptor Proteins, Vesicular Transport",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "Carrier Proteins",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "Cell Line",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "Cloning, Molecular",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "Crystallography, X-Ray",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "Escherichia coli",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "Humans",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "Hydrogen-Ion Concentration",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "Leucine",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "Models, Molecular",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "Protein Binding",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "Protein Conformation",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "Protein Structure, Tertiary",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "Receptor, IGF Type 2",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "Signal Transduction",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "Structure-Activity Relationship",
"type": "DefinedTerm"
},
{
"inDefinedTermSet": "https://www.nlm.nih.gov/mesh/",
"name": "Two-Hybrid System Techniques",
"type": "DefinedTerm"
}
],
"author": [
{
"affiliation": {
"alternateName": "Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, 20892, Bethesda, Maryland, USA",
"id": "http://www.grid.ac/institutes/grid.419635.c",
"name": [
"Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, 20892, Bethesda, Maryland, USA"
],
"type": "Organization"
},
"familyName": "Misra",
"givenName": "Saurav",
"id": "sg:person.0767342737.97",
"sameAs": [
"https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.0767342737.97"
],
"type": "Person"
},
{
"affiliation": {
"alternateName": "Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, 20892, Bethesda, Maryland, USA",
"id": "http://www.grid.ac/institutes/grid.420089.7",
"name": [
"Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, 20892, Bethesda, Maryland, USA"
],
"type": "Organization"
},
"familyName": "Puertollano",
"givenName": "Rosa",
"id": "sg:person.01220435464.58",
"sameAs": [
"https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01220435464.58"
],
"type": "Person"
},
{
"affiliation": {
"alternateName": "Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, 20892, Bethesda, Maryland, USA",
"id": "http://www.grid.ac/institutes/grid.420089.7",
"name": [
"Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, 20892, Bethesda, Maryland, USA"
],
"type": "Organization"
},
"familyName": "Kato",
"givenName": "Yukio",
"id": "sg:person.01326176201.55",
"sameAs": [
"https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.01326176201.55"
],
"type": "Person"
},
{
"affiliation": {
"alternateName": "Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, 20892, Bethesda, Maryland, USA",
"id": "http://www.grid.ac/institutes/grid.420089.7",
"name": [
"Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, 20892, Bethesda, Maryland, USA"
],
"type": "Organization"
},
"familyName": "Bonifacino",
"givenName": "Juan S.",
"id": "sg:person.0753226362.42",
"sameAs": [
"https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.0753226362.42"
],
"type": "Person"
},
{
"affiliation": {
"alternateName": "Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, 20892, Bethesda, Maryland, USA",
"id": "http://www.grid.ac/institutes/grid.419635.c",
"name": [
"Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, 20892, Bethesda, Maryland, USA"
],
"type": "Organization"
},
"familyName": "Hurley",
"givenName": "James H.",
"id": "sg:person.0642757376.69",
"sameAs": [
"https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.0642757376.69"
],
"type": "Person"
}
],
"citation": [
{
"id": "sg:pub.10.1038/81930",
"sameAs": [
"https://app.dimensions.ai/details/publication/pub.1043403844",
"https://doi.org/10.1038/81930"
],
"type": "CreativeWork"
}
],
"datePublished": "2002-02",
"datePublishedReg": "2002-02-01",
"description": "Specific sorting signals direct transmembrane proteins to the compartments of the endosomal\u2013lysosomal 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, \u03b3-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.",
"genre": "article",
"id": "sg:pub.10.1038/415933a",
"isAccessibleForFree": false,
"isFundedItemOf": [
{
"id": "sg:grant.2716321",
"type": "MonetaryGrant"
},
{
"id": "sg:grant.2718364",
"type": "MonetaryGrant"
},
{
"id": "sg:grant.2725541",
"type": "MonetaryGrant"
}
],
"isPartOf": [
{
"id": "sg:journal.1018957",
"issn": [
"0028-0836",
"1476-4687"
],
"name": "Nature",
"publisher": "Springer Nature",
"type": "Periodical"
},
{
"issueNumber": "6874",
"type": "PublicationIssue"
},
{
"type": "PublicationVolume",
"volumeNumber": "415"
}
],
"keywords": [
"mannose-6-phosphate receptor",
"VHS domain",
"critical recognition elements",
"cation-dependent mannose-6-phosphate receptor",
"shallow hydrophobic pocket",
"GGA proteins",
"dileucine sequence",
"dileucine signal",
"sorting receptor",
"transmembrane protein",
"cytoplasmic tail",
"helix 6",
"structural basis",
"Asp residues",
"hydrophobic pocket",
"specific recognition",
"extended conformation",
"protein",
"residues",
"recognition element",
"sequence",
"side chains",
"receptors",
"dileucine",
"domain",
"GGA3",
"subsites",
"high specificity",
"compartments",
"Asp",
"conformation",
"pocket",
"signals",
"tail",
"specificity",
"structure",
"recognition",
"chain",
"alignment",
"basis",
"system1",
"elements",
"GGA",
"spatial alignment"
],
"name": "Structural basis for acidic-cluster-dileucine sorting-signal recognition by VHS domains",
"pagination": "933-937",
"productId": [
{
"name": "dimensions_id",
"type": "PropertyValue",
"value": [
"pub.1023802018"
]
},
{
"name": "doi",
"type": "PropertyValue",
"value": [
"10.1038/415933a"
]
},
{
"name": "pubmed_id",
"type": "PropertyValue",
"value": [
"11859375"
]
}
],
"sameAs": [
"https://doi.org/10.1038/415933a",
"https://app.dimensions.ai/details/publication/pub.1023802018"
],
"sdDataset": "articles",
"sdDatePublished": "2022-08-04T16:54",
"sdLicense": "https://scigraph.springernature.com/explorer/license/",
"sdPublisher": {
"name": "Springer Nature - SN SciGraph project",
"type": "Organization"
},
"sdSource": "s3://com-springernature-scigraph/baseset/20220804/entities/gbq_results/article/article_357.jsonl",
"type": "ScholarlyArticle",
"url": "https://doi.org/10.1038/415933a"
}
]Download the RDF metadata as: json-ld nt turtle xml License info
JSON-LD is a popular format for linked data which is fully compatible with JSON.
curl -H 'Accept: application/ld+json' 'https://scigraph.springernature.com/pub.10.1038/415933a'
N-Triples is a line-based linked data format ideal for batch operations.
curl -H 'Accept: application/n-triples' 'https://scigraph.springernature.com/pub.10.1038/415933a'
Turtle is a human-readable linked data format.
curl -H 'Accept: text/turtle' 'https://scigraph.springernature.com/pub.10.1038/415933a'
RDF/XML is a standard XML format for linked data.
curl -H 'Accept: application/rdf+xml' 'https://scigraph.springernature.com/pub.10.1038/415933a'
This table displays all metadata directly associated to this object as RDF triples.
218 TRIPLES
21 PREDICATES
89 URIs
80 LITERALS
25 BLANK NODES